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+anno_start	anno_end	anno_text	entity_type	sentence	section
+26	31	human	species	Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase	TITLE
+32	37	Naa60	protein	Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase	TITLE
+39	43	NatF	complex_assembly	Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase	TITLE
+78	95	acetyltransferase	protein_type	Structure and function of human Naa60 (NatF), a Golgi-localized bi-functional acetyltransferase	TITLE
+0	22	N-terminal acetylation	ptm	N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains.	ABSTRACT
+24	38	Nt-acetylation	ptm	N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains.	ABSTRACT
+56	85	N-terminal acetyltransferases	protein_type	N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains.	ABSTRACT
+87	91	NATs	protein_type	N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains.	ABSTRACT
+145	152	peptide	chemical	N-terminal acetylation (Nt-acetylation), carried out by N-terminal acetyltransferases (NATs), is a conserved and primary modification of nascent peptide chains.	ABSTRACT
+0	5	Naa60	protein	Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes.	ABSTRACT
+18	22	NatF	complex_assembly	Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes.	ABSTRACT
+49	52	NAT	protein_type	Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes.	ABSTRACT
+67	91	multicellular eukaryotes	taxonomy_domain	Naa60 (also named NatF) is a recently identified NAT found only in multicellular eukaryotes.	ABSTRACT
+80	94	Nt-acetylation	ptm	This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine.	ABSTRACT
+142	169	lysine Nε-acetyltransferase	protein_type	This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine.	ABSTRACT
+171	174	KAT	protein_type	This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine.	ABSTRACT
+201	212	acetylation	ptm	This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine.	ABSTRACT
+216	222	lysine	residue_name	This protein was shown to locate on the Golgi apparatus and mainly catalyze the Nt-acetylation of transmembrane proteins, and it also harbors lysine Nε-acetyltransferase (KAT) activity to catalyze the acetylation of lysine ε-amine.	ABSTRACT
+20	38	crystal structures	evidence	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+42	47	human	species	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+48	53	Naa60	protein	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+55	61	hNaa60	protein	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+63	78	in complex with	protein_state	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+79	96	Acetyl-Coenzyme A	chemical	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+98	104	Ac-CoA	chemical	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+109	119	Coenzyme A	chemical	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+121	124	CoA	chemical	Here, we report the crystal structures of human Naa60 (hNaa60) in complex with Acetyl-Coenzyme A (Ac-CoA) or Coenzyme A (CoA).	ABSTRACT
+4	10	hNaa60	protein	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+31	48	amphipathic helix	structure_element	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+63	74	GNAT domain	structure_element	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+120	126	hNaa60	protein	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+136	149	β7-β8 hairpin	structure_element	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+189	195	hNaa60	protein	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+196	201	1-242	residue_range	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+207	220	hNaa60(1-199)	mutant	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+221	239	crystal structures	evidence	The hNaa60 protein contains an amphipathic helix following its GNAT domain that may contribute to Golgi localization of hNaa60, and the β7-β8 hairpin adopted different conformations in the hNaa60(1-242) and hNaa60(1-199) crystal structures.	ABSTRACT
+44	50	Phe 34	residue_name_number	Remarkably, we found that the side-chain of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involving enzyme, co-factor and substrates interactions.	ABSTRACT
+85	93	coenzyme	chemical	Remarkably, we found that the side-chain of Phe 34 can influence the position of the coenzyme, indicating a new regulatory mechanism involving enzyme, co-factor and substrates interactions.	ABSTRACT
+10	55	structural comparison and biochemical studies	experimental_method	Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.	ABSTRACT
+71	77	Tyr 97	residue_name_number	Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.	ABSTRACT
+82	89	His 138	residue_name_number	Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.	ABSTRACT
+141	154	non-conserved	protein_state	Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.	ABSTRACT
+155	170	β3-β4 long loop	structure_element	Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.	ABSTRACT
+205	211	hNaa60	protein	Moreover, structural comparison and biochemical studies indicated that Tyr 97 and His 138 are key residues for catalytic reaction and that a non-conserved β3-β4 long loop participates in the regulation of hNaa60 activity.	ABSTRACT
+0	11	Acetylation	ptm	Acetylation is one of the most ubiquitous modifications that plays a vital role in many biological processes, such as transcriptional regulation, protein-protein interaction, enzyme activity, protein stability, antibiotic resistance, biological rhythm and so on.	INTRO
+8	19	acetylation	ptm	Protein acetylation can be grouped into lysine Nε-acetylation and peptide N-terminal acetylation (Nt-acetylation).	INTRO
+40	61	lysine Nε-acetylation	ptm	Protein acetylation can be grouped into lysine Nε-acetylation and peptide N-terminal acetylation (Nt-acetylation).	INTRO
+66	73	peptide	chemical	Protein acetylation can be grouped into lysine Nε-acetylation and peptide N-terminal acetylation (Nt-acetylation).	INTRO
+74	96	N-terminal acetylation	ptm	Protein acetylation can be grouped into lysine Nε-acetylation and peptide N-terminal acetylation (Nt-acetylation).	INTRO
+98	112	Nt-acetylation	ptm	Protein acetylation can be grouped into lysine Nε-acetylation and peptide N-terminal acetylation (Nt-acetylation).	INTRO
+11	25	Nε-acetylation	ptm	Generally, Nε-acetylation refers to the transfer of an acetyl group from an acetyl coenzyme A (Ac-CoA) to the ε-amino group of lysine.	INTRO
+55	61	acetyl	chemical	Generally, Nε-acetylation refers to the transfer of an acetyl group from an acetyl coenzyme A (Ac-CoA) to the ε-amino group of lysine.	INTRO
+76	93	acetyl coenzyme A	chemical	Generally, Nε-acetylation refers to the transfer of an acetyl group from an acetyl coenzyme A (Ac-CoA) to the ε-amino group of lysine.	INTRO
+95	101	Ac-CoA	chemical	Generally, Nε-acetylation refers to the transfer of an acetyl group from an acetyl coenzyme A (Ac-CoA) to the ε-amino group of lysine.	INTRO
+127	133	lysine	residue_name	Generally, Nε-acetylation refers to the transfer of an acetyl group from an acetyl coenzyme A (Ac-CoA) to the ε-amino group of lysine.	INTRO
+42	67	lysine acetyltransferases	protein_type	This kind of modification is catalyzed by lysine acetyltransferases (KATs), some of which are named histone acetyltransferases (HATs) because early studies focused mostly on the post-transcriptional acetylation of histones.	INTRO
+69	73	KATs	protein_type	This kind of modification is catalyzed by lysine acetyltransferases (KATs), some of which are named histone acetyltransferases (HATs) because early studies focused mostly on the post-transcriptional acetylation of histones.	INTRO
+100	126	histone acetyltransferases	protein_type	This kind of modification is catalyzed by lysine acetyltransferases (KATs), some of which are named histone acetyltransferases (HATs) because early studies focused mostly on the post-transcriptional acetylation of histones.	INTRO
+128	132	HATs	protein_type	This kind of modification is catalyzed by lysine acetyltransferases (KATs), some of which are named histone acetyltransferases (HATs) because early studies focused mostly on the post-transcriptional acetylation of histones.	INTRO
+199	210	acetylation	ptm	This kind of modification is catalyzed by lysine acetyltransferases (KATs), some of which are named histone acetyltransferases (HATs) because early studies focused mostly on the post-transcriptional acetylation of histones.	INTRO
+214	222	histones	protein_type	This kind of modification is catalyzed by lysine acetyltransferases (KATs), some of which are named histone acetyltransferases (HATs) because early studies focused mostly on the post-transcriptional acetylation of histones.	INTRO
+61	75	Nε-acetylation	ptm	Despite the prominent accomplishments in the field regarding Nε-acetylation by KATs for over 50 years, the significance of the more evolutionarily conserved Nt-acetylation is still inconclusive.	INTRO
+79	83	KATs	protein_type	Despite the prominent accomplishments in the field regarding Nε-acetylation by KATs for over 50 years, the significance of the more evolutionarily conserved Nt-acetylation is still inconclusive.	INTRO
+157	171	Nt-acetylation	ptm	Despite the prominent accomplishments in the field regarding Nε-acetylation by KATs for over 50 years, the significance of the more evolutionarily conserved Nt-acetylation is still inconclusive.	INTRO
+0	14	Nt-acetylation	ptm	Nt-acetylation is an abundant and evolutionarily conserved modification occurring in bacteria, archaea and eukaryotes.	INTRO
+85	93	bacteria	taxonomy_domain	Nt-acetylation is an abundant and evolutionarily conserved modification occurring in bacteria, archaea and eukaryotes.	INTRO
+95	102	archaea	taxonomy_domain	Nt-acetylation is an abundant and evolutionarily conserved modification occurring in bacteria, archaea and eukaryotes.	INTRO
+107	117	eukaryotes	taxonomy_domain	Nt-acetylation is an abundant and evolutionarily conserved modification occurring in bacteria, archaea and eukaryotes.	INTRO
+45	50	human	species	It is estimated that about 80–90% of soluble human proteins and 50–70% of yeast proteins are subjected to Nt-acetylation, where an acetyl moiety is transferred from Ac-CoA to the α-amino group of the first residue.	INTRO
+74	79	yeast	taxonomy_domain	It is estimated that about 80–90% of soluble human proteins and 50–70% of yeast proteins are subjected to Nt-acetylation, where an acetyl moiety is transferred from Ac-CoA to the α-amino group of the first residue.	INTRO
+106	120	Nt-acetylation	ptm	It is estimated that about 80–90% of soluble human proteins and 50–70% of yeast proteins are subjected to Nt-acetylation, where an acetyl moiety is transferred from Ac-CoA to the α-amino group of the first residue.	INTRO
+131	137	acetyl	chemical	It is estimated that about 80–90% of soluble human proteins and 50–70% of yeast proteins are subjected to Nt-acetylation, where an acetyl moiety is transferred from Ac-CoA to the α-amino group of the first residue.	INTRO
+165	171	Ac-CoA	chemical	It is estimated that about 80–90% of soluble human proteins and 50–70% of yeast proteins are subjected to Nt-acetylation, where an acetyl moiety is transferred from Ac-CoA to the α-amino group of the first residue.	INTRO
+34	48	Nt-acetylation	ptm	Recently Nt-acetylome expands the Nt-acetylation to transmembrane proteins.	INTRO
+7	21	Nε-acetylation	ptm	Unlike Nε-acetylation that can be eliminated by deacetylases, Nt-acetylation is considered irreversible since no corresponding deacetylase is found to date.	INTRO
+48	60	deacetylases	protein_type	Unlike Nε-acetylation that can be eliminated by deacetylases, Nt-acetylation is considered irreversible since no corresponding deacetylase is found to date.	INTRO
+62	76	Nt-acetylation	ptm	Unlike Nε-acetylation that can be eliminated by deacetylases, Nt-acetylation is considered irreversible since no corresponding deacetylase is found to date.	INTRO
+91	103	irreversible	protein_state	Unlike Nε-acetylation that can be eliminated by deacetylases, Nt-acetylation is considered irreversible since no corresponding deacetylase is found to date.	INTRO
+127	138	deacetylase	protein_type	Unlike Nε-acetylation that can be eliminated by deacetylases, Nt-acetylation is considered irreversible since no corresponding deacetylase is found to date.	INTRO
+9	23	Nt-acetylation	ptm	Although Nt-acetylation has been regarded as a co-translational modification traditionally, there is evidence that post-translational Nt-acetylation exists.	INTRO
+134	148	Nt-acetylation	ptm	Although Nt-acetylation has been regarded as a co-translational modification traditionally, there is evidence that post-translational Nt-acetylation exists.	INTRO
+110	124	Nt-acetylation	ptm	During the past decades, a large number of Nt-acetylome researches have shed light on the functional roles of Nt-acetylation, including protein degradation, subcellular localization, protein-protein interaction, protein-membrane interaction, plant development, stress-response and protein stability.	INTRO
+242	247	plant	taxonomy_domain	During the past decades, a large number of Nt-acetylome researches have shed light on the functional roles of Nt-acetylation, including protein degradation, subcellular localization, protein-protein interaction, protein-membrane interaction, plant development, stress-response and protein stability.	INTRO
+4	18	Nt-acetylation	ptm	The Nt-acetylation is carried out by N-terminal acetyltransferases (NATs) that belong to the GNAT superfamily.	INTRO
+37	66	N-terminal acetyltransferases	protein_type	The Nt-acetylation is carried out by N-terminal acetyltransferases (NATs) that belong to the GNAT superfamily.	INTRO
+68	72	NATs	protein_type	The Nt-acetylation is carried out by N-terminal acetyltransferases (NATs) that belong to the GNAT superfamily.	INTRO
+93	109	GNAT superfamily	protein_type	The Nt-acetylation is carried out by N-terminal acetyltransferases (NATs) that belong to the GNAT superfamily.	INTRO
+13	17	NATs	protein_type	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+19	23	NatA	complex_assembly	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+24	25	B	complex_assembly	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+26	27	C	complex_assembly	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+28	29	D	complex_assembly	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+30	31	E	complex_assembly	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+32	33	F	complex_assembly	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+59	69	eukaryotes	taxonomy_domain	To date, six NATs (NatA/B/C/D/E/F) have been identified in eukaryotes.	INTRO
+20	34	Nt-acetylation	ptm	About 40 percent of Nt-acetylation of soluble proteins in cells is catalyzed by NatA complex which is composed of the catalytic subunit Naa10p and the auxiliary subunit Naa15p.	INTRO
+80	84	NatA	complex_assembly	About 40 percent of Nt-acetylation of soluble proteins in cells is catalyzed by NatA complex which is composed of the catalytic subunit Naa10p and the auxiliary subunit Naa15p.	INTRO
+136	142	Naa10p	protein	About 40 percent of Nt-acetylation of soluble proteins in cells is catalyzed by NatA complex which is composed of the catalytic subunit Naa10p and the auxiliary subunit Naa15p.	INTRO
+169	175	Naa15p	protein	About 40 percent of Nt-acetylation of soluble proteins in cells is catalyzed by NatA complex which is composed of the catalytic subunit Naa10p and the auxiliary subunit Naa15p.	INTRO
+0	4	NatE	complex_assembly	NatE was found to physically interact with the NatA complex without any observation of impact on NatA-activity.	INTRO
+47	51	NatA	complex_assembly	NatE was found to physically interact with the NatA complex without any observation of impact on NatA-activity.	INTRO
+97	101	NatA	complex_assembly	NatE was found to physically interact with the NatA complex without any observation of impact on NatA-activity.	INTRO
+34	38	NATs	protein_type	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+43	47	NatB	complex_assembly	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+52	56	NatC	complex_assembly	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+94	99	Naa20	protein	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+104	109	Naa30	protein	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+137	142	Naa25	protein	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+147	152	Naa35	protein	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+153	158	Naa38	protein	Two other multimeric complexes of NATs are NatB and NatC which contain the catalytic subunits Naa20 and Naa30 and the auxiliary subunits Naa25 and Naa35/Naa38, respectively.	INTRO
+41	46	Naa40	protein	Furthermore, only the catalytic subunits Naa40 and Naa60 were found for NatD and NatF, respectively.	INTRO
+51	56	Naa60	protein	Furthermore, only the catalytic subunits Naa40 and Naa60 were found for NatD and NatF, respectively.	INTRO
+72	76	NatD	complex_assembly	Furthermore, only the catalytic subunits Naa40 and Naa60 were found for NatD and NatF, respectively.	INTRO
+81	85	NatF	complex_assembly	Furthermore, only the catalytic subunits Naa40 and Naa60 were found for NatD and NatF, respectively.	INTRO
+8	22	Nt-acetylation	ptm	Besides Nt-acetylation, accumulating reports have proposed Nε-acetylation carried out by NATs.	INTRO
+59	73	Nε-acetylation	ptm	Besides Nt-acetylation, accumulating reports have proposed Nε-acetylation carried out by NATs.	INTRO
+89	93	NATs	protein_type	Besides Nt-acetylation, accumulating reports have proposed Nε-acetylation carried out by NATs.	INTRO
+53	67	Nt-acetylation	ptm	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+76	81	yeast	taxonomy_domain	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+86	91	human	species	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+147	151	NatF	complex_assembly	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+166	194	N-terminal acetyltransferase	protein_type	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+223	227	NatF	complex_assembly	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+240	245	NAA60	protein	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+264	306	Histone acetyltransferase type B protein 4	protein	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+308	312	HAT4	protein	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+315	320	Naa60	protein	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+324	346	N-acetyltransferase 15	protein	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+348	353	NAT15	protein	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+386	389	NAT	protein_type	There is an evolutionary increasing in the degree of Nt-acetylation between yeast and human which could partly be explained by the contribution of NatF. As the first N-terminal acetyltransferase discovered on an organelle, NatF, encoded by NAA60 and also named as Histone acetyltransferase type B protein 4 (HAT4), Naa60 or N-acetyltransferase 15 (NAT15), is the youngest member of the NAT family.	INTRO
+13	17	NATs	protein_type	Unlike other NATs that are highly conserved among lower and higher eukaryotes, NatF only exists in higher eukaryotes.	INTRO
+27	43	highly conserved	protein_state	Unlike other NATs that are highly conserved among lower and higher eukaryotes, NatF only exists in higher eukaryotes.	INTRO
+50	55	lower	taxonomy_domain	Unlike other NATs that are highly conserved among lower and higher eukaryotes, NatF only exists in higher eukaryotes.	INTRO
+60	77	higher eukaryotes	taxonomy_domain	Unlike other NATs that are highly conserved among lower and higher eukaryotes, NatF only exists in higher eukaryotes.	INTRO
+79	83	NatF	complex_assembly	Unlike other NATs that are highly conserved among lower and higher eukaryotes, NatF only exists in higher eukaryotes.	INTRO
+99	116	higher eukaryotes	taxonomy_domain	Unlike other NATs that are highly conserved among lower and higher eukaryotes, NatF only exists in higher eukaryotes.	INTRO
+37	41	NatF	complex_assembly	Subsequent researches indicated that NatF displays its catalytic ability with both Nt-acetylation and lysine Nε-acetylation.	INTRO
+83	97	Nt-acetylation	ptm	Subsequent researches indicated that NatF displays its catalytic ability with both Nt-acetylation and lysine Nε-acetylation.	INTRO
+102	123	lysine Nε-acetylation	ptm	Subsequent researches indicated that NatF displays its catalytic ability with both Nt-acetylation and lysine Nε-acetylation.	INTRO
+6	34	N-terminal acetyltransferase	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+36	40	NatF	complex_assembly	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+67	78	acetylation	ptm	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+187	195	Met-Lys-	structure_element	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+197	205	Met-Val-	structure_element	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+207	215	Met-Ala-	structure_element	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+220	228	Met-Met-	structure_element	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+293	297	NatC	complex_assembly	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+302	306	NatE	complex_assembly	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+327	331	NatF	complex_assembly	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+342	366	lysine acetyltransferase	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+390	408	lysine acetylation	ptm	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+417	424	histone	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+425	427	H4	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+439	441	H4	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+441	444	K20	residue_name_number	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+446	448	H4	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+448	451	K79	residue_name_number	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+456	458	H4	protein_type	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+458	461	K91	residue_name_number	As an N-terminal acetyltransferase, NatF can specifically catalyze acetylation of the N-terminal α-amine of most transmembrane proteins and has substrate preference towards proteins with Met-Lys-, Met-Val-, Met-Ala- and Met-Met-N-termini, thus partially overlapping substrate selectivity with NatC and NatE. On the other hand, NatF, with its lysine acetyltransferase activity, mediates the lysine acetylation of free histone H4, including H4K20, H4K79 and H4K91.	INTRO
+29	33	NatF	complex_assembly	Another important feature of NatF is that this protein is anchored on the Golgi apparatus through its C-terminal membrane-integrating region and takes part in the maintaining of Golgi integrity.	INTRO
+113	140	membrane-integrating region	structure_element	Another important feature of NatF is that this protein is anchored on the Golgi apparatus through its C-terminal membrane-integrating region and takes part in the maintaining of Golgi integrity.	INTRO
+81	85	NatF	complex_assembly	With its unique intracellular organellar localization and substrate selectivity, NatF appears to provide more evolutionary information among the NAT family members.	INTRO
+145	148	NAT	protein_type	With its unique intracellular organellar localization and substrate selectivity, NatF appears to provide more evolutionary information among the NAT family members.	INTRO
+27	31	NatF	complex_assembly	It was recently found that NatF facilitates nucleosomes assembly and that NAA60 knockdown in MCF7-cell inhibits cell proliferation, sensitizes cells to DNA damage and induces cell apoptosis.	INTRO
+44	55	nucleosomes	complex_assembly	It was recently found that NatF facilitates nucleosomes assembly and that NAA60 knockdown in MCF7-cell inhibits cell proliferation, sensitizes cells to DNA damage and induces cell apoptosis.	INTRO
+74	79	NAA60	protein	It was recently found that NatF facilitates nucleosomes assembly and that NAA60 knockdown in MCF7-cell inhibits cell proliferation, sensitizes cells to DNA damage and induces cell apoptosis.	INTRO
+3	13	Drosophila	taxonomy_domain	In Drosophila cells, NAA60 knockdown induces chromosomal segregation defects during anaphase including lagging chromosomes and chromosomal bridges.	INTRO
+21	26	NAA60	protein	In Drosophila cells, NAA60 knockdown induces chromosomal segregation defects during anaphase including lagging chromosomes and chromosomal bridges.	INTRO
+66	70	NatF	complex_assembly	Much recent attention has also been focused on the requirement of NatF for regulation of organellar structure.	INTRO
+15	20	NAA60	protein	In HeLa cells, NAA60 knockdown causes Golgi apparatus fragmentation which can be rescued by overexpression Naa60.	INTRO
+92	106	overexpression	experimental_method	In HeLa cells, NAA60 knockdown causes Golgi apparatus fragmentation which can be rescued by overexpression Naa60.	INTRO
+107	112	Naa60	protein	In HeLa cells, NAA60 knockdown causes Golgi apparatus fragmentation which can be rescued by overexpression Naa60.	INTRO
+79	83	NATs	protein_type	The systematic investigation of publicly available microarray data showed that NATs share distinct tissue-specific expression patterns in Drosophila and NatF shows a higher expression level in central nervous system of Drosophila.	INTRO
+138	148	Drosophila	taxonomy_domain	The systematic investigation of publicly available microarray data showed that NATs share distinct tissue-specific expression patterns in Drosophila and NatF shows a higher expression level in central nervous system of Drosophila.	INTRO
+153	157	NatF	complex_assembly	The systematic investigation of publicly available microarray data showed that NATs share distinct tissue-specific expression patterns in Drosophila and NatF shows a higher expression level in central nervous system of Drosophila.	INTRO
+219	229	Drosophila	taxonomy_domain	The systematic investigation of publicly available microarray data showed that NATs share distinct tissue-specific expression patterns in Drosophila and NatF shows a higher expression level in central nervous system of Drosophila.	INTRO
+18	24	solved	experimental_method	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+29	39	structures	evidence	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+43	48	human	species	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+49	54	Naa60	protein	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+56	60	NatF	complex_assembly	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+62	77	in complex with	protein_state	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+78	86	coenzyme	chemical	In this study, we solved the structures of human Naa60 (NatF) in complex with coenzyme.	INTRO
+4	10	hNaa60	protein	The hNaa60 protein contains a unique amphipathic α-helix (α5) following its GNAT domain that might account for the Golgi localization of this protein.	INTRO
+37	56	amphipathic α-helix	structure_element	The hNaa60 protein contains a unique amphipathic α-helix (α5) following its GNAT domain that might account for the Golgi localization of this protein.	INTRO
+58	60	α5	structure_element	The hNaa60 protein contains a unique amphipathic α-helix (α5) following its GNAT domain that might account for the Golgi localization of this protein.	INTRO
+76	87	GNAT domain	structure_element	The hNaa60 protein contains a unique amphipathic α-helix (α5) following its GNAT domain that might account for the Golgi localization of this protein.	INTRO
+0	18	Crystal structures	evidence	Crystal structures showed that the β7-β8 hairpin rotated about 50 degrees upon removing the C-terminal region of the protein and this movement substantially changed the geometry of the substrate-binding pocket.	INTRO
+35	48	β7-β8 hairpin	structure_element	Crystal structures showed that the β7-β8 hairpin rotated about 50 degrees upon removing the C-terminal region of the protein and this movement substantially changed the geometry of the substrate-binding pocket.	INTRO
+92	109	C-terminal region	structure_element	Crystal structures showed that the β7-β8 hairpin rotated about 50 degrees upon removing the C-terminal region of the protein and this movement substantially changed the geometry of the substrate-binding pocket.	INTRO
+185	209	substrate-binding pocket	site	Crystal structures showed that the β7-β8 hairpin rotated about 50 degrees upon removing the C-terminal region of the protein and this movement substantially changed the geometry of the substrate-binding pocket.	INTRO
+25	31	Phe 34	residue_name_number	Remarkably, we find that Phe 34 may participate in the proper positioning of the coenzyme for the transfer reaction to occur.	INTRO
+81	89	coenzyme	chemical	Remarkably, we find that Phe 34 may participate in the proper positioning of the coenzyme for the transfer reaction to occur.	INTRO
+8	28	structure comparison	experimental_method	Further structure comparison and biochemical studies also identified other key structural elements essential for the enzyme activity of Naa60.	INTRO
+33	52	biochemical studies	experimental_method	Further structure comparison and biochemical studies also identified other key structural elements essential for the enzyme activity of Naa60.	INTRO
+136	141	Naa60	protein	Further structure comparison and biochemical studies also identified other key structural elements essential for the enzyme activity of Naa60.	INTRO
+8	17	structure	evidence	Overall structure of hNaa60	RESULTS
+21	27	hNaa60	protein	Overall structure of hNaa60	RESULTS
+88	94	hNaa60	protein	In the effort to prepare the protein for structural studies, we tried a large number of hNaa60 constructs but all failed due to heavy precipitation or aggregation.	RESULTS
+0	18	Sequence alignment	experimental_method	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+22	27	Naa60	protein	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+62	73	Glu-Glu-Arg	structure_element	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+75	78	EER	structure_element	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+87	98	Val-Val-Pro	structure_element	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+100	103	VVP	structure_element	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+163	177	Xenopus Laevis	species	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+185	197	Homo sapiens	species	Sequence alignment of Naa60 from different species revealed a Glu-Glu-Arg (EER) versus Val-Val-Pro (VVP) sequence difference near the N-terminus of the protein in Xenopus Laevis versus Homo sapiens (Fig. 1A).	RESULTS
+169	176	mutated	experimental_method	Considering that terminal residues may lack higher-order structure and hydrophobic residues in this region may expose to solvent and hence cause protein aggregation, we mutated residues 4–6 from VVP to EER for the purpose of improving solubility of this protein.	RESULTS
+186	189	4–6	residue_range	Considering that terminal residues may lack higher-order structure and hydrophobic residues in this region may expose to solvent and hence cause protein aggregation, we mutated residues 4–6 from VVP to EER for the purpose of improving solubility of this protein.	RESULTS
+195	205	VVP to EER	mutant	Considering that terminal residues may lack higher-order structure and hydrophobic residues in this region may expose to solvent and hence cause protein aggregation, we mutated residues 4–6 from VVP to EER for the purpose of improving solubility of this protein.	RESULTS
+80	86	hNaa60	protein	According to previous studies, this N-terminal region should not interfere with hNaa60’s Golgi localization.	RESULTS
+14	20	hNaa60	protein	We tried many hNaa60 constructs with the three-residues mutation but only the truncated variant 1-199 and the full-length protein behaved well.	RESULTS
+56	64	mutation	experimental_method	We tried many hNaa60 constructs with the three-residues mutation but only the truncated variant 1-199 and the full-length protein behaved well.	RESULTS
+78	87	truncated	protein_state	We tried many hNaa60 constructs with the three-residues mutation but only the truncated variant 1-199 and the full-length protein behaved well.	RESULTS
+96	101	1-199	residue_range	We tried many hNaa60 constructs with the three-residues mutation but only the truncated variant 1-199 and the full-length protein behaved well.	RESULTS
+110	121	full-length	protein_state	We tried many hNaa60 constructs with the three-residues mutation but only the truncated variant 1-199 and the full-length protein behaved well.	RESULTS
+16	23	crystal	evidence	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+31	40	truncated	protein_state	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+49	54	1-199	residue_range	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+55	70	in complex with	protein_state	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+71	74	CoA	chemical	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+120	127	crystal	evidence	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+135	146	full-length	protein_state	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+174	179	1-242	residue_range	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+181	196	in complex with	protein_state	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+197	203	Ac-CoA	chemical	We obtained the crystal of the truncated variant 1-199 in complex with CoA first, and after extensive trials we got the crystal of the full-length protein (spanning residues 1-242) in complex with Ac-CoA (Fig. 1B,C).	RESULTS
+34	41	mutants	protein_state	Hereafter, all deletions or point mutants of hNaa60 we describe here are with the EER mutation.	RESULTS
+45	51	hNaa60	protein	Hereafter, all deletions or point mutants of hNaa60 we describe here are with the EER mutation.	RESULTS
+82	85	EER	structure_element	Hereafter, all deletions or point mutants of hNaa60 we describe here are with the EER mutation.	RESULTS
+86	94	mutation	experimental_method	Hereafter, all deletions or point mutants of hNaa60 we describe here are with the EER mutation.	RESULTS
+4	22	crystal structures	evidence	The crystal structures of hNaa60(1-242)/Ac-CoA and hNaa60(1-199)/CoA were determined by molecular replacement and refined to 1.38 Å and 1.60 Å resolution, respectively (Table 1).	RESULTS
+26	46	hNaa60(1-242)/Ac-CoA	complex_assembly	The crystal structures of hNaa60(1-242)/Ac-CoA and hNaa60(1-199)/CoA were determined by molecular replacement and refined to 1.38 Å and 1.60 Å resolution, respectively (Table 1).	RESULTS
+51	68	hNaa60(1-199)/CoA	complex_assembly	The crystal structures of hNaa60(1-242)/Ac-CoA and hNaa60(1-199)/CoA were determined by molecular replacement and refined to 1.38 Å and 1.60 Å resolution, respectively (Table 1).	RESULTS
+88	109	molecular replacement	experimental_method	The crystal structures of hNaa60(1-242)/Ac-CoA and hNaa60(1-199)/CoA were determined by molecular replacement and refined to 1.38 Å and 1.60 Å resolution, respectively (Table 1).	RESULTS
+4	25	electron density maps	evidence	The electron density maps were of sufficient quality to trace residues 1-211 of hNaa60(1-242) and residues 5-199 of hNaa60(1-199).	RESULTS
+71	76	1-211	residue_range	The electron density maps were of sufficient quality to trace residues 1-211 of hNaa60(1-242) and residues 5-199 of hNaa60(1-199).	RESULTS
+80	86	hNaa60	protein	The electron density maps were of sufficient quality to trace residues 1-211 of hNaa60(1-242) and residues 5-199 of hNaa60(1-199).	RESULTS
+87	92	1-242	residue_range	The electron density maps were of sufficient quality to trace residues 1-211 of hNaa60(1-242) and residues 5-199 of hNaa60(1-199).	RESULTS
+107	112	5-199	residue_range	The electron density maps were of sufficient quality to trace residues 1-211 of hNaa60(1-242) and residues 5-199 of hNaa60(1-199).	RESULTS
+116	129	hNaa60(1-199)	mutant	The electron density maps were of sufficient quality to trace residues 1-211 of hNaa60(1-242) and residues 5-199 of hNaa60(1-199).	RESULTS
+4	13	structure	evidence	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+17	23	hNaa60	protein	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+43	57	central domain	structure_element	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+79	111	GCN5-related N-acetyltransferase	protein_type	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+113	117	GNAT	protein_type	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+143	151	extended	protein_state	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+152	177	N- and C-terminal regions	structure_element	The structure of hNaa60 protein contains a central domain exhibiting a classic GCN5-related N-acetyltransferase (GNAT) folding, along with the extended N- and C-terminal regions (Fig. 1B,C).	RESULTS
+4	18	central domain	structure_element	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+33	42	β strands	structure_element	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+44	49	β1-β9	structure_element	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+60	69	α-helixes	structure_element	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+71	76	α1-α4	structure_element	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+85	99	highly similar	protein_state	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+113	120	hNaa50p	protein	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+140	144	NATs	protein_type	The central domain includes nine β strands (β1-β9) and four α-helixes (α1-α4) and is highly similar to the known hNaa50p and other reported NATs (Fig. 1D).	RESULTS
+12	18	hNaa60	protein	However, in hNaa60, there is an extra 20-residue loop between β3 and β4 that forms a small subdomain with well-defined 3D structure (Fig. 1B–D).	RESULTS
+32	53	extra 20-residue loop	structure_element	However, in hNaa60, there is an extra 20-residue loop between β3 and β4 that forms a small subdomain with well-defined 3D structure (Fig. 1B–D).	RESULTS
+62	64	β3	structure_element	However, in hNaa60, there is an extra 20-residue loop between β3 and β4 that forms a small subdomain with well-defined 3D structure (Fig. 1B–D).	RESULTS
+69	71	β4	structure_element	However, in hNaa60, there is an extra 20-residue loop between β3 and β4 that forms a small subdomain with well-defined 3D structure (Fig. 1B–D).	RESULTS
+85	100	small subdomain	structure_element	However, in hNaa60, there is an extra 20-residue loop between β3 and β4 that forms a small subdomain with well-defined 3D structure (Fig. 1B–D).	RESULTS
+17	30	β7-β8 strands	structure_element	Furthermore, the β7-β8 strands form an approximately antiparallel β-hairpin structure remarkably different from that in hNaa50p (Fig. 1D).	RESULTS
+39	85	approximately antiparallel β-hairpin structure	structure_element	Furthermore, the β7-β8 strands form an approximately antiparallel β-hairpin structure remarkably different from that in hNaa50p (Fig. 1D).	RESULTS
+120	127	hNaa50p	protein	Furthermore, the β7-β8 strands form an approximately antiparallel β-hairpin structure remarkably different from that in hNaa50p (Fig. 1D).	RESULTS
+4	29	N- and C-terminal regions	structure_element	The N- and C-terminal regions form helical structures (α0 and α5) stretching out from the central GCN5-domain (Fig. 1C).	RESULTS
+35	53	helical structures	structure_element	The N- and C-terminal regions form helical structures (α0 and α5) stretching out from the central GCN5-domain (Fig. 1C).	RESULTS
+55	57	α0	structure_element	The N- and C-terminal regions form helical structures (α0 and α5) stretching out from the central GCN5-domain (Fig. 1C).	RESULTS
+62	64	α5	structure_element	The N- and C-terminal regions form helical structures (α0 and α5) stretching out from the central GCN5-domain (Fig. 1C).	RESULTS
+98	109	GCN5-domain	structure_element	The N- and C-terminal regions form helical structures (α0 and α5) stretching out from the central GCN5-domain (Fig. 1C).	RESULTS
+55	61	hNaa60	protein	Interestingly, we found that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) (Figure S1), indicating that residues 200–242 may have some auto-inhibitory effect on the activity of the enzyme.	RESULTS
+62	67	1-242	residue_range	Interestingly, we found that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) (Figure S1), indicating that residues 200–242 may have some auto-inhibitory effect on the activity of the enzyme.	RESULTS
+96	109	hNaa60(1-199)	mutant	Interestingly, we found that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) (Figure S1), indicating that residues 200–242 may have some auto-inhibitory effect on the activity of the enzyme.	RESULTS
+148	155	200–242	residue_range	Interestingly, we found that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) (Figure S1), indicating that residues 200–242 may have some auto-inhibitory effect on the activity of the enzyme.	RESULTS
+50	56	hNaa60	protein	However, since this region was not visible in the hNaa60(1-242) crystal structure, we do not yet understand how this happens.	RESULTS
+57	62	1-242	residue_range	However, since this region was not visible in the hNaa60(1-242) crystal structure, we do not yet understand how this happens.	RESULTS
+64	81	crystal structure	evidence	However, since this region was not visible in the hNaa60(1-242) crystal structure, we do not yet understand how this happens.	RESULTS
+34	40	hNaa60	protein	Another possibility is that since hNaa60 is localized on Golgi apparatus, the observed low activity of the full-length hNaa60 might be related to lack of Golgi localization of the enzyme in our in vitro studies.	RESULTS
+107	118	full-length	protein_state	Another possibility is that since hNaa60 is localized on Golgi apparatus, the observed low activity of the full-length hNaa60 might be related to lack of Golgi localization of the enzyme in our in vitro studies.	RESULTS
+119	125	hNaa60	protein	Another possibility is that since hNaa60 is localized on Golgi apparatus, the observed low activity of the full-length hNaa60 might be related to lack of Golgi localization of the enzyme in our in vitro studies.	RESULTS
+48	55	mutants	protein_state	For the convenience of studying the kinetics of mutants, the mutagenesis studies described hereafter were all based on hNaa60 (1-199).	RESULTS
+61	80	mutagenesis studies	experimental_method	For the convenience of studying the kinetics of mutants, the mutagenesis studies described hereafter were all based on hNaa60 (1-199).	RESULTS
+119	133	hNaa60 (1-199)	mutant	For the convenience of studying the kinetics of mutants, the mutagenesis studies described hereafter were all based on hNaa60 (1-199).	RESULTS
+3	22	amphipathic α-helix	structure_element	An amphipathic α-helix in the C-terminal region may contribute to Golgi localization of hNaa60	RESULTS
+30	47	C-terminal region	structure_element	An amphipathic α-helix in the C-terminal region may contribute to Golgi localization of hNaa60	RESULTS
+88	94	hNaa60	protein	An amphipathic α-helix in the C-terminal region may contribute to Golgi localization of hNaa60	RESULTS
+13	19	hNaa60	protein	There is one hNaa60 molecule in the asymmetric unit in the hNaa60(1-242)/Ac-CoA structure.	RESULTS
+59	79	hNaa60(1-242)/Ac-CoA	complex_assembly	There is one hNaa60 molecule in the asymmetric unit in the hNaa60(1-242)/Ac-CoA structure.	RESULTS
+80	89	structure	evidence	There is one hNaa60 molecule in the asymmetric unit in the hNaa60(1-242)/Ac-CoA structure.	RESULTS
+4	21	C-terminal region	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+40	51	GCN5-domain	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+61	78	amphipathic helix	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+80	82	α5	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+152	176	hydrophobic interactions	bond_interaction	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+185	193	α5-helix	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+200	218	hydrophobic groove	site	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+242	244	β1	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+249	259	β3 strands	structure_element	The C-terminal region extended from the GCN5-domain forms an amphipathic helix (α5) and interacts with a molecule in a neighbor asymmetric unit through hydrophobic interactions between α5-helix and a hydrophobic groove between the N-terminal β1 and β3 strands of the neighbor molecule (Fig. 2A).	RESULTS
+4	24	C-terminal extension	structure_element	The C-terminal extension following α5-helix forms a β-turn that wraps around and interacts with the neighbor protein molecule through hydrophobic interactions, too.	RESULTS
+35	43	α5-helix	structure_element	The C-terminal extension following α5-helix forms a β-turn that wraps around and interacts with the neighbor protein molecule through hydrophobic interactions, too.	RESULTS
+52	58	β-turn	structure_element	The C-terminal extension following α5-helix forms a β-turn that wraps around and interacts with the neighbor protein molecule through hydrophobic interactions, too.	RESULTS
+134	158	hydrophobic interactions	bond_interaction	The C-terminal extension following α5-helix forms a β-turn that wraps around and interacts with the neighbor protein molecule through hydrophobic interactions, too.	RESULTS
+7	24	hNaa60(1-199)/CoA	complex_assembly	In the hNaa60(1-199)/CoA structure, a part of the α5-helix is deleted due to truncation of the C-terminal region (Fig. 1B).	RESULTS
+25	34	structure	evidence	In the hNaa60(1-199)/CoA structure, a part of the α5-helix is deleted due to truncation of the C-terminal region (Fig. 1B).	RESULTS
+50	58	α5-helix	structure_element	In the hNaa60(1-199)/CoA structure, a part of the α5-helix is deleted due to truncation of the C-terminal region (Fig. 1B).	RESULTS
+95	112	C-terminal region	structure_element	In the hNaa60(1-199)/CoA structure, a part of the α5-helix is deleted due to truncation of the C-terminal region (Fig. 1B).	RESULTS
+41	49	α5-helix	structure_element	Interestingly, the remaining residues in α5-helix still form an amphipathic helix although the hydrophobic interaction with the N-terminal hydrophobic groove of a neighbor molecule is abolished and the helix is largely exposed in solvent due to different crystal packing (Fig. 2B).	RESULTS
+64	81	amphipathic helix	structure_element	Interestingly, the remaining residues in α5-helix still form an amphipathic helix although the hydrophobic interaction with the N-terminal hydrophobic groove of a neighbor molecule is abolished and the helix is largely exposed in solvent due to different crystal packing (Fig. 2B).	RESULTS
+95	118	hydrophobic interaction	bond_interaction	Interestingly, the remaining residues in α5-helix still form an amphipathic helix although the hydrophobic interaction with the N-terminal hydrophobic groove of a neighbor molecule is abolished and the helix is largely exposed in solvent due to different crystal packing (Fig. 2B).	RESULTS
+139	157	hydrophobic groove	site	Interestingly, the remaining residues in α5-helix still form an amphipathic helix although the hydrophobic interaction with the N-terminal hydrophobic groove of a neighbor molecule is abolished and the helix is largely exposed in solvent due to different crystal packing (Fig. 2B).	RESULTS
+202	207	helix	structure_element	Interestingly, the remaining residues in α5-helix still form an amphipathic helix although the hydrophobic interaction with the N-terminal hydrophobic groove of a neighbor molecule is abolished and the helix is largely exposed in solvent due to different crystal packing (Fig. 2B).	RESULTS
+255	270	crystal packing	evidence	Interestingly, the remaining residues in α5-helix still form an amphipathic helix although the hydrophobic interaction with the N-terminal hydrophobic groove of a neighbor molecule is abolished and the helix is largely exposed in solvent due to different crystal packing (Fig. 2B).	RESULTS
+39	46	182–216	residue_range	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+85	91	hNaa60	protein	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+119	128	structure	evidence	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+134	149	solvent-exposed	protein_state	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+150	167	amphipathic helix	structure_element	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+169	171	α5	structure_element	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+192	199	190-202	residue_range	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+259	266	Ile 190	residue_name_number	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+268	275	Leu 191	residue_name_number	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+277	284	Ile 194	residue_name_number	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+286	293	Leu 197	residue_name_number	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+298	305	Leu 201	residue_name_number	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+398	404	hNaa60	protein	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+579	587	KalSec14	protein	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+589	593	Atg3	protein	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+595	601	PB1-F2	protein	A recent research showed that residues 182–216 are important for the localization of hNaa60 on Golgi. According to our structure, the solvent-exposed amphipathic helix (α5) formed by residues 190-202 with an array of hydrophobic residues located on one side (Ile 190, Leu 191, Ile 194, Leu 197 and Leu 201) and hydrophilic residues on the other side (Fig. S2) might account for interaction between hNaa60 and Golgi membrane, as it is a typical structure accounting for membrane association through immersing into the lipid bi-layer with its hydrophobic side as was observed with KalSec14, Atg3, PB1-F2 etc.	RESULTS
+4	17	β7-β8 hairpin	structure_element	The β7-β8 hairpin showed alternative conformations in the hNaa60 crystal structures	RESULTS
+58	64	hNaa60	protein	The β7-β8 hairpin showed alternative conformations in the hNaa60 crystal structures	RESULTS
+65	83	crystal structures	evidence	The β7-β8 hairpin showed alternative conformations in the hNaa60 crystal structures	RESULTS
+0	13	Superposition	experimental_method	Superposition of hNaa60(1-242)/Ac-CoA, hNaa60(1-199)/CoA and hNaa50/CoA/peptide (PDB 3TFY) revealed considerable difference in the β7-β8 hairpin region despite the overall stability and similarity of the GNAT domain (Fig. 1D).	RESULTS
+17	37	hNaa60(1-242)/Ac-CoA	complex_assembly	Superposition of hNaa60(1-242)/Ac-CoA, hNaa60(1-199)/CoA and hNaa50/CoA/peptide (PDB 3TFY) revealed considerable difference in the β7-β8 hairpin region despite the overall stability and similarity of the GNAT domain (Fig. 1D).	RESULTS
+39	56	hNaa60(1-199)/CoA	complex_assembly	Superposition of hNaa60(1-242)/Ac-CoA, hNaa60(1-199)/CoA and hNaa50/CoA/peptide (PDB 3TFY) revealed considerable difference in the β7-β8 hairpin region despite the overall stability and similarity of the GNAT domain (Fig. 1D).	RESULTS
+61	79	hNaa50/CoA/peptide	complex_assembly	Superposition of hNaa60(1-242)/Ac-CoA, hNaa60(1-199)/CoA and hNaa50/CoA/peptide (PDB 3TFY) revealed considerable difference in the β7-β8 hairpin region despite the overall stability and similarity of the GNAT domain (Fig. 1D).	RESULTS
+131	144	β7-β8 hairpin	structure_element	Superposition of hNaa60(1-242)/Ac-CoA, hNaa60(1-199)/CoA and hNaa50/CoA/peptide (PDB 3TFY) revealed considerable difference in the β7-β8 hairpin region despite the overall stability and similarity of the GNAT domain (Fig. 1D).	RESULTS
+204	215	GNAT domain	structure_element	Superposition of hNaa60(1-242)/Ac-CoA, hNaa60(1-199)/CoA and hNaa50/CoA/peptide (PDB 3TFY) revealed considerable difference in the β7-β8 hairpin region despite the overall stability and similarity of the GNAT domain (Fig. 1D).	RESULTS
+3	9	hNaa60	protein	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+10	15	1-242	residue_range	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+22	35	β7-β8 hairpin	structure_element	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+73	83	α1-α2 loop	structure_element	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+109	131	substrate binding site	site	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+145	151	hNaa50	protein	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+185	193	flexible	protein_state	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+194	198	loop	structure_element	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+213	223	β6-β7 loop	structure_element	In hNaa60(1-242), the β7-β8 hairpin is located in close proximity to the α1-α2 loop, creating a more compact substrate binding site than that in hNaa50, where this region adopts a more flexible loop conformation (β6-β7 loop).	RESULTS
+5	13	removing	experimental_method	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+18	35	C-terminal region	structure_element	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+39	45	hNaa60	protein	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+64	78	hNaa60 (1-199)	mutant	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+127	140	β7-β8 hairpin	structure_element	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+148	155	crystal	evidence	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+200	207	hairpin	structure_element	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+234	244	α1-α2 loop	structure_element	Upon removing the C-terminal region of hNaa60, we observed that hNaa60 (1-199) molecules pack in a different way involving the β7-β8 hairpin in the crystal, leading to about 50 degree rotation of the hairpin which moves away from the α1-α2 loop (Figs 1D and 2C).	RESULTS
+69	91	substrate binding site	site	This conformational change substantially altered the geometry of the substrate binding site, which could potentially change the way in which the substrate accesses the active site of the enzyme.	RESULTS
+168	179	active site	site	This conformational change substantially altered the geometry of the substrate binding site, which could potentially change the way in which the substrate accesses the active site of the enzyme.	RESULTS
+3	9	hNaa60	protein	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+10	15	1-242	residue_range	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+22	35	β7-β8 hairpin	structure_element	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+47	58	active site	site	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+96	102	hNaa50	protein	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+168	179	active site	site	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+231	237	tunnel	site	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+244	250	Ac-CoA	chemical	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+251	254	CoA	chemical	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+306	309	NAT	protein_type	In hNaa60(1-242), the β7-β8 hairpin covers the active site in a way similar to that observed in hNaa50, presumably leaving only one way for the substrate to access the active site, i.e. to enter from the opposite end into the same tunnel where Ac-CoA/CoA binds (Fig. 2D), which may accommodate access of a NAT substrate only.	RESULTS
+0	3	KAT	protein_type	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+16	22	hNaa60	protein	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+30	37	histone	protein_type	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+38	40	H4	protein_type	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+83	102	enzyme kinetic data	evidence	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+123	129	hNaa60	protein	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+144	149	H3-H4	complex_assembly	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+150	158	tetramer	oligomeric_state	KAT activity of hNaa60 toward histone H4 has been noted in previous study, and our enzyme kinetic data also indicated that hNaa60 can acetylate H3-H4 tetramer in vitro (Figure S3).	RESULTS
+29	40	acetylation	ptm	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+51	58	histone	protein_type	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+59	64	H3-H4	complex_assembly	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+65	73	tetramer	oligomeric_state	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+80	97	mass spectrometry	experimental_method	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+125	131	lysine	residue_name	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+187	198	acetylation	ptm	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+217	228	acetylation	ptm	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+257	270	hNaa60(1-199)	mutant	Furthermore, we analyzed the acetylation status of histone H3-H4 tetramer using mass spectrometry and observed that multiple lysine residues in the protein showed significantly increased acetylation level and changed acetylation profile upon treatment with hNaa60(1-199) (Figure S4).	RESULTS
+18	64	liquid chromatography-tandem mass spectrometry	experimental_method	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+66	74	LC/MS/MS	experimental_method	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+100	107	peptide	chemical	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+109	130	NH2-MKGKEEKEGGAR-COOH	chemical	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+153	166	hNaa60(1-199)	mutant	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+228	234	lysine	residue_name	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+268	278	acetylated	protein_state	We also conducted liquid chromatography-tandem mass spectrometry (LC/MS/MS) analysis on a synthetic peptide (NH2-MKGKEEKEGGAR-COOH) after treatment with hNaa60(1-199), and the data confirmed that both the N-terminal α-amine and lysine side-chain ε-amine were robustly acetylated after the treatment (Table S1).	RESULTS
+7	31	structural investigation	experimental_method	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+41	45	NATs	protein_type	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+64	74	β6-β7 loop	structure_element	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+97	110	β7-β8 hairpin	structure_element	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+114	120	hNaa60	protein	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+130	140	α1-α2 loop	structure_element	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+154	176	substrate-binding site	site	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+180	184	NATs	protein_type	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+198	204	lysine	residue_name	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+223	226	KAT	protein_type	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+262	273	active site	site	Recent structural investigation of other NATs proposed that the β6-β7 loop, corresponding to the β7-β8 hairpin in hNaa60, and the α1-α2 loop flanking the substrate-binding site of NATs, prevent the lysine side-chain of the KAT substrates from inserting into the active site.	RESULTS
+8	21	superposition	experimental_method	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+25	31	hNaa60	protein	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+32	37	1-242	residue_range	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+39	48	structure	evidence	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+60	65	Hat1p	protein	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+77	80	KAT	protein_type	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+82	97	in complex with	protein_state	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+100	107	histone	protein_type	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+108	110	H4	protein_type	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+111	118	peptide	chemical	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+164	166	H4	protein_type	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+167	174	peptide	chemical	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+178	181	KAT	protein_type	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+202	215	β7-β8 hairpin	structure_element	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+219	225	hNaa60	protein	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+226	231	1-242	residue_range	Indeed, superposition of hNaa60(1-242) structure on that of Hat1p, a typical KAT, in complex with a histone H4 peptide revealed obvious overlapping/clashing of the H4 peptide (a KAT substrate) with the β7-β8 hairpin of hNaa60(1-242) (Fig. 2D).	RESULTS
+22	35	hNaa60(1-199)	mutant	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+36	53	crystal structure	evidence	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+69	82	β7-β8 hairpin	structure_element	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+135	148	active center	site	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+199	201	H4	protein_type	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+202	209	peptide	chemical	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+262	265	KAT	protein_type	Interestingly, in the hNaa60(1-199) crystal structure, the displaced β7-β8 hairpin opened a second way for the substrate to access the active center that would readily accommodate the binding of the H4 peptide (Fig. 2E), thus implied a potential explanation for KAT activity of this enzyme from a structural biological view.	RESULTS
+15	21	hNaa60	protein	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+22	27	1-242	residue_range	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+33	39	hNaa60	protein	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+52	64	crystallized	experimental_method	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+78	91	crystal forms	evidence	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+135	148	β7-β8 hairpin	structure_element	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+200	215	crystal packing	evidence	However, since hNaa60(1-242) and hNaa60(1-199) were crystallized in different crystal forms, the observed conformational change of the β7-β8 hairpin may simply be an artifact related to the different crystal packing.	RESULTS
+12	15	KAT	protein_type	Whether the KAT substrates bind to the β7-β8 hairpin displaced conformation of the enzyme needs to be verified by further structural and functional studies.	RESULTS
+39	52	β7-β8 hairpin	structure_element	Whether the KAT substrates bind to the β7-β8 hairpin displaced conformation of the enzyme needs to be verified by further structural and functional studies.	RESULTS
+122	155	structural and functional studies	experimental_method	Whether the KAT substrates bind to the β7-β8 hairpin displaced conformation of the enzyme needs to be verified by further structural and functional studies.	RESULTS
+0	6	Phe 34	residue_name_number	Phe 34 facilitates proper positioning of the cofactor for acetyl-transfer	RESULTS
+58	64	acetyl	chemical	Phe 34 facilitates proper positioning of the cofactor for acetyl-transfer	RESULTS
+4	20	electron density	evidence	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+24	30	Phe 34	residue_name_number	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+65	85	hNaa60(1-242)/Ac-CoA	complex_assembly	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+86	95	structure	evidence	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+126	143	hNaa60(1-199)/CoA	complex_assembly	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+144	153	structure	evidence	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+186	192	Phe 34	residue_name_number	The electron density of Phe 34 side-chain is well defined in the hNaa60(1-242)/Ac-CoA structure, but becomes invisible in the hNaa60(1-199)/CoA structure, indicating displacement of the Phe 34 side-chain in the latter (Fig. 3A,B).	RESULTS
+18	26	malonate	chemical	A solvent-derived malonate molecule is found beside Phe 34 and the ethanethioate moiety of Ac-CoA in the high-resolution hNaa60(1-242)/Ac-CoA structure (Fig. 3A).	RESULTS
+52	58	Phe 34	residue_name_number	A solvent-derived malonate molecule is found beside Phe 34 and the ethanethioate moiety of Ac-CoA in the high-resolution hNaa60(1-242)/Ac-CoA structure (Fig. 3A).	RESULTS
+67	80	ethanethioate	chemical	A solvent-derived malonate molecule is found beside Phe 34 and the ethanethioate moiety of Ac-CoA in the high-resolution hNaa60(1-242)/Ac-CoA structure (Fig. 3A).	RESULTS
+91	97	Ac-CoA	chemical	A solvent-derived malonate molecule is found beside Phe 34 and the ethanethioate moiety of Ac-CoA in the high-resolution hNaa60(1-242)/Ac-CoA structure (Fig. 3A).	RESULTS
+121	141	hNaa60(1-242)/Ac-CoA	complex_assembly	A solvent-derived malonate molecule is found beside Phe 34 and the ethanethioate moiety of Ac-CoA in the high-resolution hNaa60(1-242)/Ac-CoA structure (Fig. 3A).	RESULTS
+142	151	structure	evidence	A solvent-derived malonate molecule is found beside Phe 34 and the ethanethioate moiety of Ac-CoA in the high-resolution hNaa60(1-242)/Ac-CoA structure (Fig. 3A).	RESULTS
+0	13	Superposition	experimental_method	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+22	31	structure	evidence	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+43	62	hNaa50p/CoA/peptide	complex_assembly	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+78	86	malonate	chemical	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+128	138	methionine	residue_name	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+156	163	peptide	chemical	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+176	182	Phe 34	residue_name_number	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+186	192	hNaa60	protein	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+210	216	Phe 27	residue_name_number	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+220	226	hNaa50	protein	Superposition of this structure on that of hNaa50p/CoA/peptide shows that the malonate molecule overlaps well on the N-terminal methionine of the substrate peptide and residue Phe 34 in hNaa60 overlaps well on Phe 27 in hNaa50 (Fig. 4A).	RESULTS
+22	31	structure	evidence	Interestingly, in the structure of hNaa60(1-199)/CoA, the terminal thiol of CoA adopts alternative conformations.	RESULTS
+35	52	hNaa60(1-199)/CoA	complex_assembly	Interestingly, in the structure of hNaa60(1-199)/CoA, the terminal thiol of CoA adopts alternative conformations.	RESULTS
+76	79	CoA	chemical	Interestingly, in the structure of hNaa60(1-199)/CoA, the terminal thiol of CoA adopts alternative conformations.	RESULTS
+33	38	amine	chemical	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+60	72	superimposed	experimental_method	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+73	91	hNaa50/CoA/peptide	complex_assembly	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+92	101	structure	evidence	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+128	141	ethanethioate	chemical	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+145	151	Ac-CoA	chemical	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+159	168	structure	evidence	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+172	192	hNaa60(1-242)/Ac-CoA	complex_assembly	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+223	233	α1-α2 loop	structure_element	One is to approach the substrate amine (as indicated by the superimposed hNaa50/CoA/peptide structure), similar to the terminal ethanethioate of Ac-CoA in the structure of hNaa60(1-242)/Ac-CoA; the other is to approach the α1-α2 loop and away from the substrate amine (Fig. 3B).	RESULTS
+37	53	electron density	evidence	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+130	146	electron density	evidence	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+178	184	Phe 34	residue_name_number	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+189	195	solved	experimental_method	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+200	217	crystal structure	evidence	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+221	243	hNaa60(1-199) F34A/CoA	complex_assembly	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+249	258	structure	evidence	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+267	273	mutant	protein_state	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+295	312	hNaa60(1-199)/CoA	complex_assembly	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+347	363	electron density	evidence	To rule out the possibility that the electron density we define as the alternative conformation of the thiol terminus is residual electron density of the displaced side-chain of Phe 34, we solved the crystal structure of hNaa60(1-199) F34A/CoA. The structure of this mutant is highly similar to hNaa60(1-199)/CoA and there is essentially the same electron density corresponding to the alternative conformation of the thiol (Fig. 3C).	RESULTS
+0	6	Phe 27	residue_name_number	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+10	17	hNaa50p	protein	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+33	39	Phe 34	residue_name_number	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+43	49	hNaa60	protein	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+111	121	methionine	residue_name	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+139	146	peptide	chemical	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+155	178	hydrophobic interaction	bond_interaction	Phe 27 in hNaa50p (equivalent to Phe 34 in hNaa60) has been implicated to facilitate the binding of N-terminal methionine of the substrate peptide through hydrophobic interaction.	RESULTS
+16	29	hNaa60/Ac-CoA	complex_assembly	However, in the hNaa60/Ac-CoA structure, a hydrophilic malonate molecule is found at the same location where the N-terminal methionine should bind as is indicated by the superposition (Fig. 3A), suggesting that Phe 34 may accommodate binding of hydrophilic substrate, too.	RESULTS
+30	39	structure	evidence	However, in the hNaa60/Ac-CoA structure, a hydrophilic malonate molecule is found at the same location where the N-terminal methionine should bind as is indicated by the superposition (Fig. 3A), suggesting that Phe 34 may accommodate binding of hydrophilic substrate, too.	RESULTS
+55	63	malonate	chemical	However, in the hNaa60/Ac-CoA structure, a hydrophilic malonate molecule is found at the same location where the N-terminal methionine should bind as is indicated by the superposition (Fig. 3A), suggesting that Phe 34 may accommodate binding of hydrophilic substrate, too.	RESULTS
+124	134	methionine	residue_name	However, in the hNaa60/Ac-CoA structure, a hydrophilic malonate molecule is found at the same location where the N-terminal methionine should bind as is indicated by the superposition (Fig. 3A), suggesting that Phe 34 may accommodate binding of hydrophilic substrate, too.	RESULTS
+170	183	superposition	experimental_method	However, in the hNaa60/Ac-CoA structure, a hydrophilic malonate molecule is found at the same location where the N-terminal methionine should bind as is indicated by the superposition (Fig. 3A), suggesting that Phe 34 may accommodate binding of hydrophilic substrate, too.	RESULTS
+211	217	Phe 34	residue_name_number	However, in the hNaa60/Ac-CoA structure, a hydrophilic malonate molecule is found at the same location where the N-terminal methionine should bind as is indicated by the superposition (Fig. 3A), suggesting that Phe 34 may accommodate binding of hydrophilic substrate, too.	RESULTS
+25	31	Phe 34	residue_name_number	Moreover, orientation of Phe 34 side-chain seems to be co-related to positioning of the terminus of the co-enzyme and important for placing it at a location in close proximity to the substrate amine.	RESULTS
+23	29	Phe 34	residue_name_number	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+97	100	Met	residue_name	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+113	119	mutate	experimental_method	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+128	131	Phe	residue_name	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+135	138	Ala	residue_name	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+205	211	Phe 34	residue_name_number	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+257	270	ethanethioate	chemical	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+281	287	Ac-CoA	chemical	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+293	301	mutation	experimental_method	We hypothesize that if Phe 34 only works to facilitate the binding of the hydrophobic N-terminal Met residue, to mutate it from Phe to Ala would not abolish the catalytic activity of this enzyme, while if Phe 34 also plays an essential role to position the ethanethioate moiety of Ac-CoA, the mutation would be expected to abrogate the activity of the enzyme.	RESULTS
+12	31	enzyme kinetic data	evidence	Indeed, our enzyme kinetic data showed that hNaa60(1-199) F34A mutant showed no detectable activity (Fig. 5A).	RESULTS
+44	57	hNaa60(1-199)	mutant	Indeed, our enzyme kinetic data showed that hNaa60(1-199) F34A mutant showed no detectable activity (Fig. 5A).	RESULTS
+58	62	F34A	mutant	Indeed, our enzyme kinetic data showed that hNaa60(1-199) F34A mutant showed no detectable activity (Fig. 5A).	RESULTS
+63	69	mutant	protein_state	Indeed, our enzyme kinetic data showed that hNaa60(1-199) F34A mutant showed no detectable activity (Fig. 5A).	RESULTS
+109	115	mutant	protein_state	In order to rule out the possibility that the observed loss of activity may be related to bad folding of the mutant protein, we studied the circular dichroism (CD) spectrum of the protein (Fig. 5B) and determined its crystal structure (Fig. 3C).	RESULTS
+140	158	circular dichroism	experimental_method	In order to rule out the possibility that the observed loss of activity may be related to bad folding of the mutant protein, we studied the circular dichroism (CD) spectrum of the protein (Fig. 5B) and determined its crystal structure (Fig. 3C).	RESULTS
+160	162	CD	experimental_method	In order to rule out the possibility that the observed loss of activity may be related to bad folding of the mutant protein, we studied the circular dichroism (CD) spectrum of the protein (Fig. 5B) and determined its crystal structure (Fig. 3C).	RESULTS
+164	172	spectrum	evidence	In order to rule out the possibility that the observed loss of activity may be related to bad folding of the mutant protein, we studied the circular dichroism (CD) spectrum of the protein (Fig. 5B) and determined its crystal structure (Fig. 3C).	RESULTS
+217	234	crystal structure	evidence	In order to rule out the possibility that the observed loss of activity may be related to bad folding of the mutant protein, we studied the circular dichroism (CD) spectrum of the protein (Fig. 5B) and determined its crystal structure (Fig. 3C).	RESULTS
+29	33	F34A	mutant	Both studies proved that the F34A mutant protein is well-folded.	RESULTS
+34	40	mutant	protein_state	Both studies proved that the F34A mutant protein is well-folded.	RESULTS
+52	63	well-folded	protein_state	Both studies proved that the F34A mutant protein is well-folded.	RESULTS
+50	60	α1-α2 loop	structure_element	Many studies have addressed the crucial effect of α1-α2 loop on catalysis, showing that some residues located in this area are involved in the binding of substrates.	RESULTS
+16	22	Phe 34	residue_name_number	We propose that Phe 34 may play a dual role both in interacting with the peptide substrate (recognition) and in positioning of the ethanethioate moiety of Ac-CoA to the right location to facilitate acetyl-transfer.	RESULTS
+73	80	peptide	chemical	We propose that Phe 34 may play a dual role both in interacting with the peptide substrate (recognition) and in positioning of the ethanethioate moiety of Ac-CoA to the right location to facilitate acetyl-transfer.	RESULTS
+131	144	ethanethioate	chemical	We propose that Phe 34 may play a dual role both in interacting with the peptide substrate (recognition) and in positioning of the ethanethioate moiety of Ac-CoA to the right location to facilitate acetyl-transfer.	RESULTS
+155	161	Ac-CoA	chemical	We propose that Phe 34 may play a dual role both in interacting with the peptide substrate (recognition) and in positioning of the ethanethioate moiety of Ac-CoA to the right location to facilitate acetyl-transfer.	RESULTS
+198	204	acetyl	chemical	We propose that Phe 34 may play a dual role both in interacting with the peptide substrate (recognition) and in positioning of the ethanethioate moiety of Ac-CoA to the right location to facilitate acetyl-transfer.	RESULTS
+21	27	hNaa60	protein	Structural basis for hNaa60 substrate binding	RESULTS
+70	76	hNaa60	protein	Several studies have demonstrated that the substrate specificities of hNaa60 and hNaa50 are highly overlapped.	RESULTS
+81	87	hNaa50	protein	Several studies have demonstrated that the substrate specificities of hNaa60 and hNaa50 are highly overlapped.	RESULTS
+4	13	structure	evidence	The structure of hNaa50p/CoA/peptide provides detailed information about the position of substrate N-terminal residues in the active site of hNaa50.	RESULTS
+17	36	hNaa50p/CoA/peptide	complex_assembly	The structure of hNaa50p/CoA/peptide provides detailed information about the position of substrate N-terminal residues in the active site of hNaa50.	RESULTS
+126	137	active site	site	The structure of hNaa50p/CoA/peptide provides detailed information about the position of substrate N-terminal residues in the active site of hNaa50.	RESULTS
+141	147	hNaa50	protein	The structure of hNaa50p/CoA/peptide provides detailed information about the position of substrate N-terminal residues in the active site of hNaa50.	RESULTS
+14	25	active site	site	Comparing the active site of hNaa60(1-242)/Ac-CoA with hNaa50p/CoA/peptide revealed that key catalytic and substrate binding residues are highly conserved in both proteins (Fig. 4A).	RESULTS
+29	49	hNaa60(1-242)/Ac-CoA	complex_assembly	Comparing the active site of hNaa60(1-242)/Ac-CoA with hNaa50p/CoA/peptide revealed that key catalytic and substrate binding residues are highly conserved in both proteins (Fig. 4A).	RESULTS
+55	74	hNaa50p/CoA/peptide	complex_assembly	Comparing the active site of hNaa60(1-242)/Ac-CoA with hNaa50p/CoA/peptide revealed that key catalytic and substrate binding residues are highly conserved in both proteins (Fig. 4A).	RESULTS
+93	133	catalytic and substrate binding residues	site	Comparing the active site of hNaa60(1-242)/Ac-CoA with hNaa50p/CoA/peptide revealed that key catalytic and substrate binding residues are highly conserved in both proteins (Fig. 4A).	RESULTS
+138	154	highly conserved	protein_state	Comparing the active site of hNaa60(1-242)/Ac-CoA with hNaa50p/CoA/peptide revealed that key catalytic and substrate binding residues are highly conserved in both proteins (Fig. 4A).	RESULTS
+27	34	hNaa50p	protein	With respect to catalysis, hNaa50p has been shown to employ residues Tyr 73 and His 112 to abstract proton from the α-amino group from the substrate’s first residue through a well-ordered water.	RESULTS
+69	75	Tyr 73	residue_name_number	With respect to catalysis, hNaa50p has been shown to employ residues Tyr 73 and His 112 to abstract proton from the α-amino group from the substrate’s first residue through a well-ordered water.	RESULTS
+80	87	His 112	residue_name_number	With respect to catalysis, hNaa50p has been shown to employ residues Tyr 73 and His 112 to abstract proton from the α-amino group from the substrate’s first residue through a well-ordered water.	RESULTS
+175	187	well-ordered	protein_state	With respect to catalysis, hNaa50p has been shown to employ residues Tyr 73 and His 112 to abstract proton from the α-amino group from the substrate’s first residue through a well-ordered water.	RESULTS
+188	193	water	chemical	With respect to catalysis, hNaa50p has been shown to employ residues Tyr 73 and His 112 to abstract proton from the α-amino group from the substrate’s first residue through a well-ordered water.	RESULTS
+2	14	well-ordered	protein_state	A well-ordered water was also found between Tyr 97 and His 138 in hNaa60 (1-199)/CoA and hNaa60 (1-242)/Ac-CoA (Fig. 4B).	RESULTS
+15	20	water	chemical	A well-ordered water was also found between Tyr 97 and His 138 in hNaa60 (1-199)/CoA and hNaa60 (1-242)/Ac-CoA (Fig. 4B).	RESULTS
+44	50	Tyr 97	residue_name_number	A well-ordered water was also found between Tyr 97 and His 138 in hNaa60 (1-199)/CoA and hNaa60 (1-242)/Ac-CoA (Fig. 4B).	RESULTS
+55	62	His 138	residue_name_number	A well-ordered water was also found between Tyr 97 and His 138 in hNaa60 (1-199)/CoA and hNaa60 (1-242)/Ac-CoA (Fig. 4B).	RESULTS
+66	84	hNaa60 (1-199)/CoA	complex_assembly	A well-ordered water was also found between Tyr 97 and His 138 in hNaa60 (1-199)/CoA and hNaa60 (1-242)/Ac-CoA (Fig. 4B).	RESULTS
+89	110	hNaa60 (1-242)/Ac-CoA	complex_assembly	A well-ordered water was also found between Tyr 97 and His 138 in hNaa60 (1-199)/CoA and hNaa60 (1-242)/Ac-CoA (Fig. 4B).	RESULTS
+29	35	Tyr 97	residue_name_number	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+40	47	His 138	residue_name_number	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+51	57	hNaa60	protein	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+72	79	mutated	experimental_method	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+98	105	alanine	residue_name	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+110	123	phenylalanine	residue_name	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+168	175	mutants	protein_state	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+188	202	kinetic assays	experimental_method	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+207	218	well-folded	protein_state	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+222	224	CD	experimental_method	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+225	232	spectra	evidence	To determine the function of Tyr 97 and His 138 in hNaa60 catalysis, we mutated these residues to alanine and phenylalanine, respectively, and confirmed that all these mutants used in our kinetic assays are well-folded by CD spectra (Fig. 5B).	RESULTS
+45	53	SDS-PAGE	experimental_method	Purity of all proteins were also analyzed by SDS-PAGE (Figure S5).	RESULTS
+24	31	mutants	protein_state	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+32	36	Y97A	mutant	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+38	42	Y97F	mutant	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+44	49	H138A	mutant	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+54	59	H138F	mutant	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+60	82	abolished the activity	protein_state	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+86	92	hNaa60	protein	As show in Fig. 5A, the mutants Y97A, Y97F, H138A and H138F abolished the activity of hNaa60.	RESULTS
+16	22	mutate	experimental_method	In contrast, to mutate the nearby solvent exposed residue Glu 37 to Ala (E37A) has little impact on the activity of hNaa60 (Figs 4B and 5A).	RESULTS
+34	49	solvent exposed	protein_state	In contrast, to mutate the nearby solvent exposed residue Glu 37 to Ala (E37A) has little impact on the activity of hNaa60 (Figs 4B and 5A).	RESULTS
+58	64	Glu 37	residue_name_number	In contrast, to mutate the nearby solvent exposed residue Glu 37 to Ala (E37A) has little impact on the activity of hNaa60 (Figs 4B and 5A).	RESULTS
+68	71	Ala	residue_name	In contrast, to mutate the nearby solvent exposed residue Glu 37 to Ala (E37A) has little impact on the activity of hNaa60 (Figs 4B and 5A).	RESULTS
+73	77	E37A	mutant	In contrast, to mutate the nearby solvent exposed residue Glu 37 to Ala (E37A) has little impact on the activity of hNaa60 (Figs 4B and 5A).	RESULTS
+116	122	hNaa60	protein	In contrast, to mutate the nearby solvent exposed residue Glu 37 to Ala (E37A) has little impact on the activity of hNaa60 (Figs 4B and 5A).	RESULTS
+19	52	structural and functional studies	experimental_method	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+67	73	hNaa60	protein	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+118	124	Tyr 97	residue_name_number	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+126	133	His 138	residue_name_number	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+140	152	well-ordered	protein_state	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+153	158	water	chemical	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+180	186	hNaa50	protein	In conclusion, the structural and functional studies indicate that hNaa60 applies the same two base mechanism through Tyr 97, His 138 and a well-ordered water as was described for hNaa50.	RESULTS
+4	12	malonate	chemical	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+38	58	hNaa60(1-242)/Ac-CoA	complex_assembly	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+59	76	crystal structure	evidence	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+132	138	hNaa60	protein	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+166	177	active site	site	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+206	209	Met	residue_name	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+227	234	peptide	chemical	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+242	255	superposition	experimental_method	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+265	284	hNaa50p/CoA/peptide	complex_assembly	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+285	294	structure	evidence	The malonate molecule observed in the hNaa60(1-242)/Ac-CoA crystal structure may be indicative of the substrate binding position of hNaa60 since it is located in the active site and overlaps the N-terminal Met of the substrate peptide in the superposition with the hNaa50p/CoA/peptide structure (Fig. 4A).	RESULTS
+9	15	Tyr 38	residue_name_number	Residues Tyr 38, Asn 143 and Tyr 165 are located around the malonate and interact with it through direct hydrogen bonds or water bridge (Fig. 4C).	RESULTS
+17	24	Asn 143	residue_name_number	Residues Tyr 38, Asn 143 and Tyr 165 are located around the malonate and interact with it through direct hydrogen bonds or water bridge (Fig. 4C).	RESULTS
+29	36	Tyr 165	residue_name_number	Residues Tyr 38, Asn 143 and Tyr 165 are located around the malonate and interact with it through direct hydrogen bonds or water bridge (Fig. 4C).	RESULTS
+60	68	malonate	chemical	Residues Tyr 38, Asn 143 and Tyr 165 are located around the malonate and interact with it through direct hydrogen bonds or water bridge (Fig. 4C).	RESULTS
+105	119	hydrogen bonds	bond_interaction	Residues Tyr 38, Asn 143 and Tyr 165 are located around the malonate and interact with it through direct hydrogen bonds or water bridge (Fig. 4C).	RESULTS
+123	135	water bridge	bond_interaction	Residues Tyr 38, Asn 143 and Tyr 165 are located around the malonate and interact with it through direct hydrogen bonds or water bridge (Fig. 4C).	RESULTS
+9	17	malonate	chemical	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+73	79	lysine	residue_name	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+91	98	peptide	chemical	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+125	149	hydrophilic interactions	bond_interaction	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+223	229	Tyr 38	residue_name_number	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+231	238	Asn 143	residue_name_number	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+243	250	Tyr 165	residue_name_number	Although malonate is negatively charged, which is different from that of lysine ε-amine or peptide N-terminal amine, similar hydrophilic interactions may take place when substrate amine presents in the same position, since Tyr 38, Asn 143 and Tyr 165 are not positively or negatively charged.	RESULTS
+57	61	Y38A	mutant	In agreement with this hypothesis, it was found that the Y38A, N143A and Y165A mutants all showed remarkably reduced activities as compared to WT, implying that these residues may be critical for substrate binding (Figs 4C and 5A).	RESULTS
+63	68	N143A	mutant	In agreement with this hypothesis, it was found that the Y38A, N143A and Y165A mutants all showed remarkably reduced activities as compared to WT, implying that these residues may be critical for substrate binding (Figs 4C and 5A).	RESULTS
+73	78	Y165A	mutant	In agreement with this hypothesis, it was found that the Y38A, N143A and Y165A mutants all showed remarkably reduced activities as compared to WT, implying that these residues may be critical for substrate binding (Figs 4C and 5A).	RESULTS
+79	86	mutants	protein_state	In agreement with this hypothesis, it was found that the Y38A, N143A and Y165A mutants all showed remarkably reduced activities as compared to WT, implying that these residues may be critical for substrate binding (Figs 4C and 5A).	RESULTS
+143	145	WT	protein_state	In agreement with this hypothesis, it was found that the Y38A, N143A and Y165A mutants all showed remarkably reduced activities as compared to WT, implying that these residues may be critical for substrate binding (Figs 4C and 5A).	RESULTS
+4	14	β3-β4 loop	structure_element	The β3-β4 loop participates in the regulation of hNaa60-activity	RESULTS
+49	55	hNaa60	protein	The β3-β4 loop participates in the regulation of hNaa60-activity	RESULTS
+17	19	β3	structure_element	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+24	26	β4	structure_element	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+30	36	hNaa60	protein	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+51	71	20-residue long loop	structure_element	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+82	87	73–92	residue_range	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+99	109	short turn	structure_element	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+124	127	NAT	protein_type	Residues between β3 and β4 of hNaa60 form a unique 20-residue long loop (residues 73–92) that is a short turn in many other NAT members (Fig. 1D).	RESULTS
+30	46	auto-acetylation	ptm	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+50	56	hNaa60	protein	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+56	59	K79	residue_name_number	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+92	98	hNaa60	protein	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+142	148	Lys 79	residue_name_number	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+152	162	acetylated	protein_state	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+170	188	crystal structures	evidence	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+216	232	electron density	evidence	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+236	242	Lys 79	residue_name_number	Previous study indicated that auto-acetylation of hNaa60K79 could influence the activity of hNaa60; however, we were not able to determine if Lys 79 is acetylated in our crystal structures due to poor quality of the electron density of Lys 79 side-chain.	RESULTS
+18	35	mass spectrometry	experimental_method	We therefore used mass spectrometry to analyze if Lys 79 was acetylated in our bacterially purified proteins, and observed no modification on this residue (Figure S6).	RESULTS
+50	56	Lys 79	residue_name_number	We therefore used mass spectrometry to analyze if Lys 79 was acetylated in our bacterially purified proteins, and observed no modification on this residue (Figure S6).	RESULTS
+61	71	acetylated	protein_state	We therefore used mass spectrometry to analyze if Lys 79 was acetylated in our bacterially purified proteins, and observed no modification on this residue (Figure S6).	RESULTS
+24	30	hNaa60	protein	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+30	33	K79	residue_name_number	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+34	50	auto-acetylation	ptm	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+79	83	K79R	mutant	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+88	92	K79Q	mutant	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+93	100	mutants	protein_state	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+117	130	un-acetylated	protein_state	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+135	145	acetylated	protein_state	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+154	160	Lys 79	residue_name_number	To assess the impact of hNaa60K79 auto-acetylation, we studied the kinetics of K79R and K79Q mutants which mimic the un-acetylated and acetylated form of Lys 79, respectively.	RESULTS
+20	24	K79R	mutant	Interestingly, both K79R and K79Q mutants led to an increase in the catalytic activity of hNaa60, while K79A mutant led to modest decrease of the activity (Fig. 5A).	RESULTS
+29	33	K79Q	mutant	Interestingly, both K79R and K79Q mutants led to an increase in the catalytic activity of hNaa60, while K79A mutant led to modest decrease of the activity (Fig. 5A).	RESULTS
+34	41	mutants	protein_state	Interestingly, both K79R and K79Q mutants led to an increase in the catalytic activity of hNaa60, while K79A mutant led to modest decrease of the activity (Fig. 5A).	RESULTS
+90	96	hNaa60	protein	Interestingly, both K79R and K79Q mutants led to an increase in the catalytic activity of hNaa60, while K79A mutant led to modest decrease of the activity (Fig. 5A).	RESULTS
+104	108	K79A	mutant	Interestingly, both K79R and K79Q mutants led to an increase in the catalytic activity of hNaa60, while K79A mutant led to modest decrease of the activity (Fig. 5A).	RESULTS
+109	115	mutant	protein_state	Interestingly, both K79R and K79Q mutants led to an increase in the catalytic activity of hNaa60, while K79A mutant led to modest decrease of the activity (Fig. 5A).	RESULTS
+29	40	acetylation	ptm	These data indicate that the acetylation of Lys 79 is not required for optimal catalytic activity of hNaa60 in vitro.	RESULTS
+44	50	Lys 79	residue_name_number	These data indicate that the acetylation of Lys 79 is not required for optimal catalytic activity of hNaa60 in vitro.	RESULTS
+101	107	hNaa60	protein	These data indicate that the acetylation of Lys 79 is not required for optimal catalytic activity of hNaa60 in vitro.	RESULTS
+21	31	β3-β4 loop	structure_element	It is noted that the β3-β4 loop of hNaa60 acts like a door leaf to partly cover the substrate-binding pathway.	RESULTS
+35	41	hNaa60	protein	It is noted that the β3-β4 loop of hNaa60 acts like a door leaf to partly cover the substrate-binding pathway.	RESULTS
+84	109	substrate-binding pathway	site	It is noted that the β3-β4 loop of hNaa60 acts like a door leaf to partly cover the substrate-binding pathway.	RESULTS
+30	40	β3-β4 loop	structure_element	We hence hypothesize that the β3-β4 loop may interfere with the access of the peptide substrates and that the solvent-exposing Lys 79 may play a potential role to remove the door leaf when it hovers in solvent (Fig. 4D).	RESULTS
+78	85	peptide	chemical	We hence hypothesize that the β3-β4 loop may interfere with the access of the peptide substrates and that the solvent-exposing Lys 79 may play a potential role to remove the door leaf when it hovers in solvent (Fig. 4D).	RESULTS
+110	126	solvent-exposing	protein_state	We hence hypothesize that the β3-β4 loop may interfere with the access of the peptide substrates and that the solvent-exposing Lys 79 may play a potential role to remove the door leaf when it hovers in solvent (Fig. 4D).	RESULTS
+127	133	Lys 79	residue_name_number	We hence hypothesize that the β3-β4 loop may interfere with the access of the peptide substrates and that the solvent-exposing Lys 79 may play a potential role to remove the door leaf when it hovers in solvent (Fig. 4D).	RESULTS
+16	22	Glu 80	residue_name_number	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+24	30	Asp 81	residue_name_number	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+35	41	Asp 83	residue_name_number	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+56	63	His 138	residue_name_number	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+65	72	His 159	residue_name_number	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+77	84	His 158	residue_name_number	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+121	131	β3-β4 loop	structure_element	Acidic residues Glu 80, Asp 81 and Asp 83 interact with His 138, His 159 and His 158 to maintain the conformation of the β3-β4 loop, thus contribute to control the substrate binding (Fig. 4D).	RESULTS
+30	37	mutated	experimental_method	To verify this hypothesis, we mutated Glu 80, Asp 81 and Asp 83 to Ala respectively.	RESULTS
+38	44	Glu 80	residue_name_number	To verify this hypothesis, we mutated Glu 80, Asp 81 and Asp 83 to Ala respectively.	RESULTS
+46	52	Asp 81	residue_name_number	To verify this hypothesis, we mutated Glu 80, Asp 81 and Asp 83 to Ala respectively.	RESULTS
+57	63	Asp 83	residue_name_number	To verify this hypothesis, we mutated Glu 80, Asp 81 and Asp 83 to Ala respectively.	RESULTS
+67	70	Ala	residue_name	To verify this hypothesis, we mutated Glu 80, Asp 81 and Asp 83 to Ala respectively.	RESULTS
+29	33	E80A	mutant	In line with our hypothesis, E80A, D81A and D83A mutants exhibit at least 2-fold increase in hNaa60-activity (Fig. 5A).	RESULTS
+35	39	D81A	mutant	In line with our hypothesis, E80A, D81A and D83A mutants exhibit at least 2-fold increase in hNaa60-activity (Fig. 5A).	RESULTS
+44	48	D83A	mutant	In line with our hypothesis, E80A, D81A and D83A mutants exhibit at least 2-fold increase in hNaa60-activity (Fig. 5A).	RESULTS
+49	56	mutants	protein_state	In line with our hypothesis, E80A, D81A and D83A mutants exhibit at least 2-fold increase in hNaa60-activity (Fig. 5A).	RESULTS
+93	99	hNaa60	protein	In line with our hypothesis, E80A, D81A and D83A mutants exhibit at least 2-fold increase in hNaa60-activity (Fig. 5A).	RESULTS
+19	28	structure	evidence	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+45	48	NAT	protein_type	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+54	69	S. solfataricus	species	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+86	111	10-residue long extension	structure_element	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+120	122	β3	structure_element	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+127	129	β4	structure_element	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+139	172	structure and biochemical studies	experimental_method	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+189	198	extension	structure_element	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+202	207	SsNat	protein	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+254	265	active site	site	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+281	286	SsNat	protein	Interestingly, the structure of an ancestral NAT from S. solfataricus also exhibits a 10-residue long extension between β3 and β4, and the structure and biochemical studies showed that the extension of SsNat has the ability to stabilize structure of the active site and potentiate SsNat-activity.	RESULTS
+0	14	Nt-acetylation	ptm	Nt-acetylation, which is carried out by the NAT family acetyltransferases, is an ancient and essential modification of proteins.	DISCUSS
+44	73	NAT family acetyltransferases	protein_type	Nt-acetylation, which is carried out by the NAT family acetyltransferases, is an ancient and essential modification of proteins.	DISCUSS
+14	18	NATs	protein_type	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+23	39	highly conserved	protein_state	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+45	50	lower	taxonomy_domain	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+54	71	higher eukaryotes	taxonomy_domain	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+195	217	N-terminal acetylation	ptm	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+223	228	lower	taxonomy_domain	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+232	249	higher eukaryotes	taxonomy_domain	Although many NATs are highly conserved from lower to higher eukaryotes and the substrate bias of them appears to be partially overlapped, there is a significant increase in the overall level of N-terminal acetylation from lower to higher eukaryotes.	DISCUSS
+50	55	Naa60	protein	In this study we provide structural insights into Naa60 found only in multicellular eukaryotes.	DISCUSS
+70	94	multicellular eukaryotes	taxonomy_domain	In this study we provide structural insights into Naa60 found only in multicellular eukaryotes.	DISCUSS
+18	24	hNaa60	protein	The N-terminus of hNaa60 harbors three hydrophobic residues (VVP) that makes it very difficult to express and purify the protein.	DISCUSS
+61	64	VVP	structure_element	The N-terminus of hNaa60 harbors three hydrophobic residues (VVP) that makes it very difficult to express and purify the protein.	DISCUSS
+27	36	replacing	experimental_method	This problem was solved by replacing residues 4–6 from VVP to EER that are found in Naa60 from Xenopus Laevis.	DISCUSS
+46	49	4–6	residue_range	This problem was solved by replacing residues 4–6 from VVP to EER that are found in Naa60 from Xenopus Laevis.	DISCUSS
+55	58	VVP	structure_element	This problem was solved by replacing residues 4–6 from VVP to EER that are found in Naa60 from Xenopus Laevis.	DISCUSS
+62	65	EER	structure_element	This problem was solved by replacing residues 4–6 from VVP to EER that are found in Naa60 from Xenopus Laevis.	DISCUSS
+84	89	Naa60	protein	This problem was solved by replacing residues 4–6 from VVP to EER that are found in Naa60 from Xenopus Laevis.	DISCUSS
+95	109	Xenopus Laevis	species	This problem was solved by replacing residues 4–6 from VVP to EER that are found in Naa60 from Xenopus Laevis.	DISCUSS
+6	11	Naa60	protein	Since Naa60 from human and from Xenopus Laevis are highly homologous (Fig. 1A), we speculate that these two proteins should have the same biological function.	DISCUSS
+17	22	human	species	Since Naa60 from human and from Xenopus Laevis are highly homologous (Fig. 1A), we speculate that these two proteins should have the same biological function.	DISCUSS
+32	46	Xenopus Laevis	species	Since Naa60 from human and from Xenopus Laevis are highly homologous (Fig. 1A), we speculate that these two proteins should have the same biological function.	DISCUSS
+51	68	highly homologous	protein_state	Since Naa60 from human and from Xenopus Laevis are highly homologous (Fig. 1A), we speculate that these two proteins should have the same biological function.	DISCUSS
+33	43	VVP to EER	mutant	Therefore it is deduced that the VVP to EER replacement on the N-terminus of hNaa60 may not interfere with its function.	DISCUSS
+44	55	replacement	experimental_method	Therefore it is deduced that the VVP to EER replacement on the N-terminus of hNaa60 may not interfere with its function.	DISCUSS
+77	83	hNaa60	protein	Therefore it is deduced that the VVP to EER replacement on the N-terminus of hNaa60 may not interfere with its function.	DISCUSS
+16	22	hNaa60	protein	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+23	28	1-242	residue_range	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+30	39	structure	evidence	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+65	84	α-helical structure	structure_element	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+126	127	6	residue_number	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+131	138	proline	residue_name	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+161	174	hNaa60(1-199)	mutant	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+175	184	structure	evidence	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+219	241	semi-helical structure	structure_element	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+276	291	crystal packing	evidence	However, in the hNaa60(1-242) structure the N-terminus adopts an α-helical structure which will probably be kinked if residue 6 is proline (Fig. 1C), and in the hNaa60(1-199) structure the N-terminus adopts a different semi-helical structure (Fig. 1B) likely due to different crystal packing.	DISCUSS
+47	56	wild-type	protein_state	Hence it is not clear if the N-terminal end of wild-type hNaa60 is an α-helix, and what roles the hydrophobic residues 4–6 play in structure and function of wild-type hNaa60.	DISCUSS
+57	63	hNaa60	protein	Hence it is not clear if the N-terminal end of wild-type hNaa60 is an α-helix, and what roles the hydrophobic residues 4–6 play in structure and function of wild-type hNaa60.	DISCUSS
+70	77	α-helix	structure_element	Hence it is not clear if the N-terminal end of wild-type hNaa60 is an α-helix, and what roles the hydrophobic residues 4–6 play in structure and function of wild-type hNaa60.	DISCUSS
+119	122	4–6	residue_range	Hence it is not clear if the N-terminal end of wild-type hNaa60 is an α-helix, and what roles the hydrophobic residues 4–6 play in structure and function of wild-type hNaa60.	DISCUSS
+157	166	wild-type	protein_state	Hence it is not clear if the N-terminal end of wild-type hNaa60 is an α-helix, and what roles the hydrophobic residues 4–6 play in structure and function of wild-type hNaa60.	DISCUSS
+167	173	hNaa60	protein	Hence it is not clear if the N-terminal end of wild-type hNaa60 is an α-helix, and what roles the hydrophobic residues 4–6 play in structure and function of wild-type hNaa60.	DISCUSS
+33	41	mutation	experimental_method	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+43	46	VVP	structure_element	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+50	53	EER	structure_element	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+81	87	hNaa60	protein	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+113	124	full-length	protein_state	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+141	150	truncated	protein_state	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+159	164	1-199	residue_range	In addition to the three-residue mutation (VVP to EER), we also tried many other hNaa60 constructs, but only the full-length protein and the truncated variant 1-199 behaved well.	DISCUSS
+43	49	hNaa60	protein	The finding that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) is intriguing.	DISCUSS
+50	55	1-242	residue_range	The finding that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) is intriguing.	DISCUSS
+84	97	hNaa60(1-199)	mutant	The finding that the catalytic activity of hNaa60(1-242) is much lower than that of hNaa60(1-199) is intriguing.	DISCUSS
+38	49	full-length	protein_state	We speculate that low activity of the full-length hNaa60 might be related to lack of Golgi localization of the enzyme in our in vitro studies or there remains some undiscovered auto-inhibitory regulation in the full-length protein.	DISCUSS
+50	56	hNaa60	protein	We speculate that low activity of the full-length hNaa60 might be related to lack of Golgi localization of the enzyme in our in vitro studies or there remains some undiscovered auto-inhibitory regulation in the full-length protein.	DISCUSS
+211	222	full-length	protein_state	We speculate that low activity of the full-length hNaa60 might be related to lack of Golgi localization of the enzyme in our in vitro studies or there remains some undiscovered auto-inhibitory regulation in the full-length protein.	DISCUSS
+4	10	hNaa60	protein	The hNaa60 protein was proven to be localized on Golgi apparatus.	DISCUSS
+41	62	transmembrane domains	structure_element	Aksnes and colleagues predicted putative transmembrane domains and two putative sites of S-palmitoylation, by bioinformatics means, to account for Golgi localization of the protein.	DISCUSS
+89	105	S-palmitoylation	ptm	Aksnes and colleagues predicted putative transmembrane domains and two putative sites of S-palmitoylation, by bioinformatics means, to account for Golgi localization of the protein.	DISCUSS
+10	17	mutated	experimental_method	They then mutated all five cysteine residues of hNaa60’s to serine, including the two putative S-palmitoylation sites.	DISCUSS
+27	35	cysteine	residue_name	They then mutated all five cysteine residues of hNaa60’s to serine, including the two putative S-palmitoylation sites.	DISCUSS
+48	54	hNaa60	protein	They then mutated all five cysteine residues of hNaa60’s to serine, including the two putative S-palmitoylation sites.	DISCUSS
+60	66	serine	residue_name	They then mutated all five cysteine residues of hNaa60’s to serine, including the two putative S-palmitoylation sites.	DISCUSS
+95	117	S-palmitoylation sites	site	They then mutated all five cysteine residues of hNaa60’s to serine, including the two putative S-palmitoylation sites.	DISCUSS
+15	24	mutations	experimental_method	However, these mutations did not abolish Naa60 membrane localization, indicating that S-palmitoylation is unlikely to (solely) account for targeting hNaa60 on Golgi.	DISCUSS
+41	46	Naa60	protein	However, these mutations did not abolish Naa60 membrane localization, indicating that S-palmitoylation is unlikely to (solely) account for targeting hNaa60 on Golgi.	DISCUSS
+86	102	S-palmitoylation	ptm	However, these mutations did not abolish Naa60 membrane localization, indicating that S-palmitoylation is unlikely to (solely) account for targeting hNaa60 on Golgi.	DISCUSS
+149	155	hNaa60	protein	However, these mutations did not abolish Naa60 membrane localization, indicating that S-palmitoylation is unlikely to (solely) account for targeting hNaa60 on Golgi.	DISCUSS
+13	19	adding	experimental_method	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+29	36	217–242	residue_range	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+40	46	hNaa60	protein	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+68	75	217–236	residue_range	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+97	118	transmembrane domains	structure_element	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+141	145	eGFP	experimental_method	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+216	220	eGFP	experimental_method	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+221	234	hNaa60182-242	mutant	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+279	286	182–216	residue_range	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+327	333	hNaa60	protein	Furthermore, adding residues 217–242 of hNaa60 (containing residues 217–236, one of the putative transmembrane domains) to the C terminus of eGFP were not sufficient to localize the protein on Golgi apparatus, while eGFP-hNaa60182-242 was sufficient to, suggesting that residues 182–216 are important for Golgi localization of hNaa60.	DISCUSS
+23	30	190–202	residue_range	We found that residues 190–202 formed an amphipathic helix with an array of hydrophobic residues located on one side.	DISCUSS
+41	58	amphipathic helix	structure_element	We found that residues 190–202 formed an amphipathic helix with an array of hydrophobic residues located on one side.	DISCUSS
+76	95	amphipathic helices	structure_element	This observation is reminiscent of the protein/membrane interaction through amphipathic helices in the cases of KalSec14, Atg3, PB1-F2 etc.	DISCUSS
+112	120	KalSec14	protein	This observation is reminiscent of the protein/membrane interaction through amphipathic helices in the cases of KalSec14, Atg3, PB1-F2 etc.	DISCUSS
+122	126	Atg3	protein	This observation is reminiscent of the protein/membrane interaction through amphipathic helices in the cases of KalSec14, Atg3, PB1-F2 etc.	DISCUSS
+128	134	PB1-F2	protein	This observation is reminiscent of the protein/membrane interaction through amphipathic helices in the cases of KalSec14, Atg3, PB1-F2 etc.	DISCUSS
+17	34	amphipathic helix	structure_element	In this model an amphipathic helix can immerse its hydrophobic side into the lipid bilayer through hydrophobic interactions.	DISCUSS
+99	123	hydrophobic interactions	bond_interaction	In this model an amphipathic helix can immerse its hydrophobic side into the lipid bilayer through hydrophobic interactions.	DISCUSS
+30	47	amphipathic helix	structure_element	Therefore we propose that the amphipathic helix α5 may contribute to Golgi localization of hNaa60.	DISCUSS
+48	50	α5	structure_element	Therefore we propose that the amphipathic helix α5 may contribute to Golgi localization of hNaa60.	DISCUSS
+91	97	hNaa60	protein	Therefore we propose that the amphipathic helix α5 may contribute to Golgi localization of hNaa60.	DISCUSS
+43	46	NAT	protein_type	Previous studies indicated that members of NAT family are bi-functional NAT and KAT enzymes.	DISCUSS
+72	75	NAT	protein_type	Previous studies indicated that members of NAT family are bi-functional NAT and KAT enzymes.	DISCUSS
+80	83	KAT	protein_type	Previous studies indicated that members of NAT family are bi-functional NAT and KAT enzymes.	DISCUSS
+15	25	structures	evidence	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+29	33	NATs	protein_type	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+81	94	β6-β7 hairpin	structure_element	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+95	99	loop	structure_element	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+111	115	NATs	protein_type	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+150	184	tunnel-like substrate-binding site	site	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+194	204	α1-α2 loop	structure_element	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+234	237	NAT	protein_type	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+246	249	KAT	protein_type	However, known structures of NATs do not well support this hypothesis, since the β6-β7 hairpin/loop of most of NATs is involved in the formation of a tunnel-like substrate-binding site with the α1-α2 loop, which would be good for the NAT but not KAT activity of the enzyme.	DISCUSS
+0	15	Kinetic studies	experimental_method	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+51	54	NAT	protein_type	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+59	62	KAT	protein_type	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+75	81	hNaa50	protein	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+114	117	NAT	protein_type	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+130	135	Naa50	protein	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+156	159	KAT	protein_type	Kinetic studies have been conducted to compare the NAT and KAT activity of hNaa50 in vitro, and indicate that the NAT activity of Naa50 is much higher than KAT activity.	DISCUSS
+56	59	KAT	protein_type	However, the substrate used in this study for assessing KAT activity was a small peptide which could not really mimic the 3D structure of a folded protein substrate in vivo.	DISCUSS
+81	88	peptide	chemical	However, the substrate used in this study for assessing KAT activity was a small peptide which could not really mimic the 3D structure of a folded protein substrate in vivo.	DISCUSS
+122	134	3D structure	evidence	However, the substrate used in this study for assessing KAT activity was a small peptide which could not really mimic the 3D structure of a folded protein substrate in vivo.	DISCUSS
+140	146	folded	protein_state	However, the substrate used in this study for assessing KAT activity was a small peptide which could not really mimic the 3D structure of a folded protein substrate in vivo.	DISCUSS
+4	21	mass spectrometry	experimental_method	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+22	26	data	evidence	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+60	71	acetylation	ptm	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+75	82	histone	protein_type	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+83	88	H3-H4	complex_assembly	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+89	97	tetramer	oligomeric_state	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+98	105	lysines	residue_name	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+115	137	N-terminal acetylation	ptm	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+142	160	lysine acetylation	ptm	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+168	175	peptide	chemical	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+188	202	activity assay	experimental_method	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+223	226	KAT	protein_type	Our mass spectrometry data indicated that there were robust acetylation of histone H3-H4 tetramer lysines and both N-terminal acetylation and lysine acetylation of the peptide used in the activity assay, thus confirmed the KAT activity of this enzyme in vitro.	DISCUSS
+29	42	β7-β8 hairpin	structure_element	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+65	75	β6-β7 loop	structure_element	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+85	89	NATs	protein_type	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+107	117	structures	evidence	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+178	181	NAT	protein_type	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+182	185	KAT	protein_type	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+328	335	hairpin	structure_element	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+368	383	crystal packing	evidence	Conformational change of the β7-β8 hairpin (corresponding to the β6-β7 loop of other NATs) is noted in our structures (Figs 1D and 2C), which might provide an explanation to the NAT/KAT dual-activity in a structural biological view, but we were unable to rule out the possibility that the observed conformational change of this hairpin might be an artifact related to crystal packing or truncation of the C-terminal end of the protein.	DISCUSS
+69	72	KAT	protein_type	Further studies are therefore needed to reveal the mechanism for the KAT activity of this enzyme.	DISCUSS
+48	78	GCN5 histone acetyltransferase	protein_type	In early years, researchers found adjustment of GCN5 histone acetyltransferase structure when it binds CoA molecule.	DISCUSS
+79	88	structure	evidence	In early years, researchers found adjustment of GCN5 histone acetyltransferase structure when it binds CoA molecule.	DISCUSS
+103	106	CoA	chemical	In early years, researchers found adjustment of GCN5 histone acetyltransferase structure when it binds CoA molecule.	DISCUSS
+4	13	complexed	protein_state	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+22	26	NatA	complex_assembly	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+80	90	α1-α2 loop	structure_element	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+158	180	substrate-binding site	site	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+208	213	Naa15	protein	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+229	234	Naa10	protein	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+240	249	catalytic	protein_state	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+250	257	subunit	structure_element	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+261	265	NatA	complex_assembly	The complexed form of NatA is more suitable for catalytic activation, since the α1-α2 loop undergoes a conformation change to participate in the formation of substrate-binding site when the auxiliary subunit Naa15 interacts with Naa10 (the catalytic subunit of NatA).	DISCUSS
+7	16	structure	evidence	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+20	38	hNaa50/CoA/peptide	complex_assembly	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+40	46	Phe 27	residue_name_number	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+54	64	α1-α2 loop	structure_element	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+81	104	hydrophobic interaction	bond_interaction	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+125	128	Met	residue_name	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+142	149	peptide	chemical	In the structure of hNaa50/CoA/peptide, Phe 27 in the α1-α2 loop appears to make hydrophobic interaction with the N-terminal Met of substrate peptide.	DISCUSS
+13	33	hNaa60(1-242)/Ac-CoA	complex_assembly	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+34	51	crystal structure	evidence	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+86	92	hNaa60	protein	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+94	100	Phe 34	residue_name_number	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+154	162	malonate	chemical	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+181	203	substrate binding site	site	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+269	275	hNaa50	protein	However, the hNaa60(1-242)/Ac-CoA crystal structure indicated that its counterpart in hNaa60, Phe 34, could also accommodate the binding of a hydrophilic malonate that occupied the substrate binding site although it maintained the same conformation as that observed in hNaa50.	DISCUSS
+28	33	thiol	chemical	Interestingly, the terminal thiol of CoA adopted alternative conformations in the structure of hNaa60(1-199)/CoA. One was to approach the substrate amine; the other was to approach the α1-α2 loop and away from the substrate amine.	DISCUSS
+37	40	CoA	chemical	Interestingly, the terminal thiol of CoA adopted alternative conformations in the structure of hNaa60(1-199)/CoA. One was to approach the substrate amine; the other was to approach the α1-α2 loop and away from the substrate amine.	DISCUSS
+82	91	structure	evidence	Interestingly, the terminal thiol of CoA adopted alternative conformations in the structure of hNaa60(1-199)/CoA. One was to approach the substrate amine; the other was to approach the α1-α2 loop and away from the substrate amine.	DISCUSS
+95	112	hNaa60(1-199)/CoA	complex_assembly	Interestingly, the terminal thiol of CoA adopted alternative conformations in the structure of hNaa60(1-199)/CoA. One was to approach the substrate amine; the other was to approach the α1-α2 loop and away from the substrate amine.	DISCUSS
+185	195	α1-α2 loop	structure_element	Interestingly, the terminal thiol of CoA adopted alternative conformations in the structure of hNaa60(1-199)/CoA. One was to approach the substrate amine; the other was to approach the α1-α2 loop and away from the substrate amine.	DISCUSS
+34	37	CoA	chemical	Same alternative conformations of CoA were observed in the hNaa60(1-199)(F34A) crystal structure, and our kinetic data showed that the F34A mutation abolished the activity of the enzyme.	DISCUSS
+59	78	hNaa60(1-199)(F34A)	mutant	Same alternative conformations of CoA were observed in the hNaa60(1-199)(F34A) crystal structure, and our kinetic data showed that the F34A mutation abolished the activity of the enzyme.	DISCUSS
+79	96	crystal structure	evidence	Same alternative conformations of CoA were observed in the hNaa60(1-199)(F34A) crystal structure, and our kinetic data showed that the F34A mutation abolished the activity of the enzyme.	DISCUSS
+106	118	kinetic data	evidence	Same alternative conformations of CoA were observed in the hNaa60(1-199)(F34A) crystal structure, and our kinetic data showed that the F34A mutation abolished the activity of the enzyme.	DISCUSS
+135	139	F34A	mutant	Same alternative conformations of CoA were observed in the hNaa60(1-199)(F34A) crystal structure, and our kinetic data showed that the F34A mutation abolished the activity of the enzyme.	DISCUSS
+140	148	mutation	experimental_method	Same alternative conformations of CoA were observed in the hNaa60(1-199)(F34A) crystal structure, and our kinetic data showed that the F34A mutation abolished the activity of the enzyme.	DISCUSS
+40	46	Phe 34	residue_name_number	Taken together, our data indicated that Phe 34 in hNaa60 may play a role in placing co-enzyme at the right location to facilitate the acetyl-transfer.	DISCUSS
+50	56	hNaa60	protein	Taken together, our data indicated that Phe 34 in hNaa60 may play a role in placing co-enzyme at the right location to facilitate the acetyl-transfer.	DISCUSS
+134	140	acetyl	chemical	Taken together, our data indicated that Phe 34 in hNaa60 may play a role in placing co-enzyme at the right location to facilitate the acetyl-transfer.	DISCUSS
+59	65	Phe 34	residue_name_number	However, these data did not rule out that possibility that Phe 34 may coordinate the binding of the N-terminal Met through hydrophobic interaction as was proposed by previous studies.	DISCUSS
+111	114	Met	residue_name	However, these data did not rule out that possibility that Phe 34 may coordinate the binding of the N-terminal Met through hydrophobic interaction as was proposed by previous studies.	DISCUSS
+123	146	hydrophobic interaction	bond_interaction	However, these data did not rule out that possibility that Phe 34 may coordinate the binding of the N-terminal Met through hydrophobic interaction as was proposed by previous studies.	DISCUSS
+28	34	hNaa60	protein	Furthermore, we showed that hNaa60 adopts the classical two base mechanism to catalyze acetyl-transfer.	DISCUSS
+87	93	acetyl	chemical	Furthermore, we showed that hNaa60 adopts the classical two base mechanism to catalyze acetyl-transfer.	DISCUSS
+35	41	hNaa60	protein	Although sequence identity between hNaa60 and hNaa50 is low, key residues in the active site of both enzymes are highly conserved.	DISCUSS
+46	52	hNaa50	protein	Although sequence identity between hNaa60 and hNaa50 is low, key residues in the active site of both enzymes are highly conserved.	DISCUSS
+81	92	active site	site	Although sequence identity between hNaa60 and hNaa50 is low, key residues in the active site of both enzymes are highly conserved.	DISCUSS
+113	129	highly conserved	protein_state	Although sequence identity between hNaa60 and hNaa50 is low, key residues in the active site of both enzymes are highly conserved.	DISCUSS
+82	88	hNaa60	protein	This can reasonably explain the high overlapping substrates specificities between hNaa60 and hNaa50.	DISCUSS
+93	99	hNaa50	protein	This can reasonably explain the high overlapping substrates specificities between hNaa60 and hNaa50.	DISCUSS
+30	36	hNaa60	protein	Another structural feature of hNaa60 that distinguishes it from other NATs is the β3-β4 long loop which appears to inhibit the catalytic activity of hNaa60.	DISCUSS
+70	74	NATs	protein_type	Another structural feature of hNaa60 that distinguishes it from other NATs is the β3-β4 long loop which appears to inhibit the catalytic activity of hNaa60.	DISCUSS
+82	97	β3-β4 long loop	structure_element	Another structural feature of hNaa60 that distinguishes it from other NATs is the β3-β4 long loop which appears to inhibit the catalytic activity of hNaa60.	DISCUSS
+149	155	hNaa60	protein	Another structural feature of hNaa60 that distinguishes it from other NATs is the β3-β4 long loop which appears to inhibit the catalytic activity of hNaa60.	DISCUSS
+14	18	loop	structure_element	However, this loop also seems to stabilize the whole hNaa60 structure, because deletion mutations of this region led to protein precipitation and aggregation (Figure S7).	DISCUSS
+53	59	hNaa60	protein	However, this loop also seems to stabilize the whole hNaa60 structure, because deletion mutations of this region led to protein precipitation and aggregation (Figure S7).	DISCUSS
+60	69	structure	evidence	However, this loop also seems to stabilize the whole hNaa60 structure, because deletion mutations of this region led to protein precipitation and aggregation (Figure S7).	DISCUSS
+79	97	deletion mutations	experimental_method	However, this loop also seems to stabilize the whole hNaa60 structure, because deletion mutations of this region led to protein precipitation and aggregation (Figure S7).	DISCUSS
+36	52	auto-acetylation	ptm	A previous study suggested that the auto-acetylation of Lys 79 was important for hNaa60-activity, whereas the point mutation K79R did not decrease the activity of hNaa60 in our study.	DISCUSS
+56	62	Lys 79	residue_name_number	A previous study suggested that the auto-acetylation of Lys 79 was important for hNaa60-activity, whereas the point mutation K79R did not decrease the activity of hNaa60 in our study.	DISCUSS
+81	87	hNaa60	protein	A previous study suggested that the auto-acetylation of Lys 79 was important for hNaa60-activity, whereas the point mutation K79R did not decrease the activity of hNaa60 in our study.	DISCUSS
+110	124	point mutation	experimental_method	A previous study suggested that the auto-acetylation of Lys 79 was important for hNaa60-activity, whereas the point mutation K79R did not decrease the activity of hNaa60 in our study.	DISCUSS
+125	129	K79R	mutant	A previous study suggested that the auto-acetylation of Lys 79 was important for hNaa60-activity, whereas the point mutation K79R did not decrease the activity of hNaa60 in our study.	DISCUSS
+163	169	hNaa60	protein	A previous study suggested that the auto-acetylation of Lys 79 was important for hNaa60-activity, whereas the point mutation K79R did not decrease the activity of hNaa60 in our study.	DISCUSS
+14	30	electron density	evidence	Meanwhile, no electron density of acetyl group was found on Lys 79 in our structures and mass spectrometry analysis.	DISCUSS
+34	40	acetyl	chemical	Meanwhile, no electron density of acetyl group was found on Lys 79 in our structures and mass spectrometry analysis.	DISCUSS
+60	66	Lys 79	residue_name_number	Meanwhile, no electron density of acetyl group was found on Lys 79 in our structures and mass spectrometry analysis.	DISCUSS
+74	84	structures	evidence	Meanwhile, no electron density of acetyl group was found on Lys 79 in our structures and mass spectrometry analysis.	DISCUSS
+89	106	mass spectrometry	experimental_method	Meanwhile, no electron density of acetyl group was found on Lys 79 in our structures and mass spectrometry analysis.	DISCUSS
+27	43	auto-acetylation	ptm	Hence, it appears that the auto-acetylation of hNaa60 is not an essential modification for its activity for the protein we used here.	DISCUSS
+47	53	hNaa60	protein	Hence, it appears that the auto-acetylation of hNaa60 is not an essential modification for its activity for the protein we used here.	DISCUSS
+22	26	K79R	mutant	As for the reason why K79R in Yang’s previous studies reduced the activity of the enzyme, but in our studies it didn’t, we suspect that the stability of this mutant may play some role.	DISCUSS
+158	164	mutant	protein_state	As for the reason why K79R in Yang’s previous studies reduced the activity of the enzyme, but in our studies it didn’t, we suspect that the stability of this mutant may play some role.	DISCUSS
+0	4	K79R	mutant	K79R is less stable than the wild-type enzyme as was judged by its poorer gel-filtration behavior and tendency to precipitate.	DISCUSS
+13	19	stable	protein_state	K79R is less stable than the wild-type enzyme as was judged by its poorer gel-filtration behavior and tendency to precipitate.	DISCUSS
+29	38	wild-type	protein_state	K79R is less stable than the wild-type enzyme as was judged by its poorer gel-filtration behavior and tendency to precipitate.	DISCUSS
+74	88	gel-filtration	experimental_method	K79R is less stable than the wild-type enzyme as was judged by its poorer gel-filtration behavior and tendency to precipitate.	DISCUSS
+151	165	kinetic assays	experimental_method	In our studies we have paid special attention and carefully handled this protein to ensure that we did get enough of the protein in good condition for kinetic assays.	DISCUSS
+107	113	hNaa60	protein	The intracellular environment is more complicated than our in vitro assay and the substrate specificity of hNaa60 most focuses on transmembrane proteins.	DISCUSS
+24	30	hNaa60	protein	The interaction between hNaa60 and its substrates may involve the protein-membrane interaction which would further increase the complexity.	DISCUSS
+23	32	structure	evidence	It is not clear if the structure of hNaa60 is different in vivo or if other potential partner proteins may help to regulate its activity.	DISCUSS
+36	42	hNaa60	protein	It is not clear if the structure of hNaa60 is different in vivo or if other potential partner proteins may help to regulate its activity.	DISCUSS
+129	132	NAT	protein_type	Nevertheless, our study may be an inspiration for further studies on the functions and regulation of this youngest member of the NAT family.	DISCUSS
+8	17	structure	evidence	Overall structure of Naa60.	FIG
+21	26	Naa60	protein	Overall structure of Naa60.	FIG
+4	22	Sequence alignment	experimental_method	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+26	31	Naa60	protein	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+33	37	NatF	complex_assembly	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+39	43	HAT4	protein	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+78	90	Homo sapiens	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+92	96	Homo	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+99	108	Bos mutus	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+110	113	Bos	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+116	127	Salmo salar	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+129	134	Salmo	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+140	147	Xenopus	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+149	157	Silurana	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+159	169	tropicalis	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+171	178	Xenopus	species	(A) Sequence alignment of Naa60 (NatF, HAT4) from different species including Homo sapiens (Homo), Bos mutus (Bos), Salmo salar (Salmo) and Xenopus (Silurana) tropicalis (Xenopus).	FIG
+0	9	Alignment	experimental_method	Alignment was generated using NPS@ and ESPript.3.0 (http://espript.ibcp.fr/ESPript/ESPript/).	FIG
+9	12	4–6	residue_range	Residues 4–6 are highlighted in red box.	FIG
+8	17	structure	evidence	(B) The structure of hNaa60(1-199)/CoA complex is shown as a yellow cartoon model.	FIG
+21	38	hNaa60(1-199)/CoA	complex_assembly	(B) The structure of hNaa60(1-199)/CoA complex is shown as a yellow cartoon model.	FIG
+4	7	CoA	chemical	The CoA molecule is shown as sticks. (C) The structure of hNaa60(1-242)/Ac-CoA complex is presented as a cartoon model in cyan.	FIG
+45	54	structure	evidence	The CoA molecule is shown as sticks. (C) The structure of hNaa60(1-242)/Ac-CoA complex is presented as a cartoon model in cyan.	FIG
+58	78	hNaa60(1-242)/Ac-CoA	complex_assembly	The CoA molecule is shown as sticks. (C) The structure of hNaa60(1-242)/Ac-CoA complex is presented as a cartoon model in cyan.	FIG
+4	10	Ac-CoA	chemical	The Ac-CoA and malonate molecules are shown as cyan and purple sticks, respectively.	FIG
+15	23	malonate	chemical	The Ac-CoA and malonate molecules are shown as cyan and purple sticks, respectively.	FIG
+51	53	α0	structure_element	The secondary structures are labeled starting with α0. (D) Superposition of hNaa60(1-242) (cyan), hNaa60(1-199) (yellow) and hNaa50 (pink, PDB 3TFY).	FIG
+59	72	Superposition	experimental_method	The secondary structures are labeled starting with α0. (D) Superposition of hNaa60(1-242) (cyan), hNaa60(1-199) (yellow) and hNaa50 (pink, PDB 3TFY).	FIG
+76	82	hNaa60	protein	The secondary structures are labeled starting with α0. (D) Superposition of hNaa60(1-242) (cyan), hNaa60(1-199) (yellow) and hNaa50 (pink, PDB 3TFY).	FIG
+83	88	1-242	residue_range	The secondary structures are labeled starting with α0. (D) Superposition of hNaa60(1-242) (cyan), hNaa60(1-199) (yellow) and hNaa50 (pink, PDB 3TFY).	FIG
+98	111	hNaa60(1-199)	mutant	The secondary structures are labeled starting with α0. (D) Superposition of hNaa60(1-242) (cyan), hNaa60(1-199) (yellow) and hNaa50 (pink, PDB 3TFY).	FIG
+125	131	hNaa50	protein	The secondary structures are labeled starting with α0. (D) Superposition of hNaa60(1-242) (cyan), hNaa60(1-199) (yellow) and hNaa50 (pink, PDB 3TFY).	FIG
+4	10	Ac-CoA	chemical	The Ac-CoA of hNaa60(1-242)/Ac-CoA complex is represented as cyan sticks.	FIG
+14	34	hNaa60(1-242)/Ac-CoA	complex_assembly	The Ac-CoA of hNaa60(1-242)/Ac-CoA complex is represented as cyan sticks.	FIG
+0	14	Amphipathicity	protein_state	Amphipathicity of the α5 helix and alternative conformations of the β7-β8 hairpin.	FIG
+22	30	α5 helix	structure_element	Amphipathicity of the α5 helix and alternative conformations of the β7-β8 hairpin.	FIG
+68	81	β7-β8 hairpin	structure_element	Amphipathicity of the α5 helix and alternative conformations of the β7-β8 hairpin.	FIG
+8	16	α5 helix	structure_element	(A) The α5 helix of hNaa60(1-242) in one asymmetric unit (slate) interacts with another hNaa60 molecule in a neighboring asymmetric unit (cyan).	FIG
+20	26	hNaa60	protein	(A) The α5 helix of hNaa60(1-242) in one asymmetric unit (slate) interacts with another hNaa60 molecule in a neighboring asymmetric unit (cyan).	FIG
+27	32	1-242	residue_range	(A) The α5 helix of hNaa60(1-242) in one asymmetric unit (slate) interacts with another hNaa60 molecule in a neighboring asymmetric unit (cyan).	FIG
+88	94	hNaa60	protein	(A) The α5 helix of hNaa60(1-242) in one asymmetric unit (slate) interacts with another hNaa60 molecule in a neighboring asymmetric unit (cyan).	FIG
+39	47	α5 helix	structure_element	Side-chains of hydrophobic residues on α5 helix and the neighboring molecule participating in the interaction are shown as yellow and green sticks, respectively. (B) The α5 helix of hNaa60(1-199) in one asymmetric unit (yellow) interacts with another hNaa60 molecule in the neighboring asymmetric units (green).	FIG
+170	178	α5 helix	structure_element	Side-chains of hydrophobic residues on α5 helix and the neighboring molecule participating in the interaction are shown as yellow and green sticks, respectively. (B) The α5 helix of hNaa60(1-199) in one asymmetric unit (yellow) interacts with another hNaa60 molecule in the neighboring asymmetric units (green).	FIG
+182	195	hNaa60(1-199)	mutant	Side-chains of hydrophobic residues on α5 helix and the neighboring molecule participating in the interaction are shown as yellow and green sticks, respectively. (B) The α5 helix of hNaa60(1-199) in one asymmetric unit (yellow) interacts with another hNaa60 molecule in the neighboring asymmetric units (green).	FIG
+251	257	hNaa60	protein	Side-chains of hydrophobic residues on α5 helix and the neighboring molecule participating in the interaction are shown as yellow and green sticks, respectively. (B) The α5 helix of hNaa60(1-199) in one asymmetric unit (yellow) interacts with another hNaa60 molecule in the neighboring asymmetric units (green).	FIG
+39	47	α5 helix	structure_element	Side-chains of hydrophobic residues on α5 helix and the neighboring molecule (green) participating in the interaction are shown as yellow and green sticks, respectively.	FIG
+62	70	α5 helix	structure_element	The third molecule (pink) does not directly interact with the α5 helix.	FIG
+4	17	Superposition	experimental_method	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+21	34	hNaa60(1-199)	mutant	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+48	54	hNaa60	protein	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+55	60	1-242	residue_range	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+106	119	β7-β8 hairpin	structure_element	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+133	143	structures	evidence	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+151	164	Superposition	experimental_method	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+168	173	Hat1p	protein	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+174	176	H4	protein_type	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+210	216	hNaa60	protein	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+217	222	1-242	residue_range	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+237	250	hNaa60(1-199)	mutant	(C) Superposition of hNaa60(1-199) (yellow) and hNaa60(1-242) (cyan) showing conformational change of the β7-β8 hairpin in these two structures. (D,E) Superposition of Hat1p/H4 (gray, drawn from PDB 4PSW) with hNaa60(1-242) (cyan, D) or hNaa60(1-199) (yellow, E).	FIG
+4	11	histone	protein_type	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+12	14	H4	protein_type	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+15	22	peptide	chemical	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+26	29	KAT	protein_type	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+41	49	bound to	protein_state	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+50	55	Hat1p	protein	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+92	99	peptide	chemical	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+100	108	bound to	protein_state	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+109	115	hNaa50	protein	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+119	122	NAT	protein_type	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+175	185	Nt-peptide	chemical	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+193	206	superimposing	experimental_method	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+207	213	hNaa50	protein	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+239	245	hNaa60	protein	The histone H4 peptide (a KAT substrate) bound to Hat1p is shown in purple (D,E), while the peptide bound to hNaa50 (a NAT substrate, drawn from PDB 3TFY) is shown in orange (Nt-peptide) after superimposing hNaa50 (not shown in figure) on hNaa60 (D).	FIG
+19	22	NAT	protein_type	The α-amine of the NAT substrate and ε-amine of the KAT substrate (along with the lysine side-chain) subject to acetylation are shown as sticks.	FIG
+52	55	KAT	protein_type	The α-amine of the NAT substrate and ε-amine of the KAT substrate (along with the lysine side-chain) subject to acetylation are shown as sticks.	FIG
+82	88	lysine	residue_name	The α-amine of the NAT substrate and ε-amine of the KAT substrate (along with the lysine side-chain) subject to acetylation are shown as sticks.	FIG
+112	123	acetylation	ptm	The α-amine of the NAT substrate and ε-amine of the KAT substrate (along with the lysine side-chain) subject to acetylation are shown as sticks.	FIG
+0	20	Electron density map	evidence	Electron density map of the active site.	FIG
+28	39	active site	site	Electron density map of the active site.	FIG
+4	15	2Fo-Fc maps	evidence	The 2Fo-Fc maps contoured at 1.0σ are shown for hNaa60(1-242)/Ac-CoA (A), hNaa60(1-199)/CoA (B) and hNaa60(1-199) F34A/CoA (C).	FIG
+48	68	hNaa60(1-242)/Ac-CoA	complex_assembly	The 2Fo-Fc maps contoured at 1.0σ are shown for hNaa60(1-242)/Ac-CoA (A), hNaa60(1-199)/CoA (B) and hNaa60(1-199) F34A/CoA (C).	FIG
+74	91	hNaa60(1-199)/CoA	complex_assembly	The 2Fo-Fc maps contoured at 1.0σ are shown for hNaa60(1-242)/Ac-CoA (A), hNaa60(1-199)/CoA (B) and hNaa60(1-199) F34A/CoA (C).	FIG
+100	122	hNaa60(1-199) F34A/CoA	complex_assembly	The 2Fo-Fc maps contoured at 1.0σ are shown for hNaa60(1-242)/Ac-CoA (A), hNaa60(1-199)/CoA (B) and hNaa60(1-199) F34A/CoA (C).	FIG
+13	43	substrate peptide binding site	site	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+64	71	peptide	chemical	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+104	122	hNaa50/CoA/peptide	complex_assembly	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+131	140	structure	evidence	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+147	160	superimposing	experimental_method	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+161	167	hNaa50	protein	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+175	181	hNaa60	protein	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+182	192	structures	evidence	The putative substrate peptide binding site is indicated by the peptide (shown as pink sticks) from the hNaa50/CoA/peptide complex structure after superimposing hNaa50 on the hNaa60 structures determined in this study.	FIG
+45	54	first Met	residue_name_number	The black arrow indicates the α-amine of the first Met (M1) (all panels).	FIG
+56	58	M1	residue_name_number	The black arrow indicates the α-amine of the first Met (M1) (all panels).	FIG
+31	37	acetyl	chemical	The purple arrow indicates the acetyl moiety of Ac-CoA (A).	FIG
+48	54	Ac-CoA	chemical	The purple arrow indicates the acetyl moiety of Ac-CoA (A).	FIG
+95	101	Phe 34	residue_name_number	The red arrow indicates the alternative conformation of the thiol moiety of the co-enzyme when Phe 34 side-chain is displaced (B) or mutated to Ala (C).	FIG
+133	140	mutated	experimental_method	The red arrow indicates the alternative conformation of the thiol moiety of the co-enzyme when Phe 34 side-chain is displaced (B) or mutated to Ala (C).	FIG
+144	147	Ala	residue_name	The red arrow indicates the alternative conformation of the thiol moiety of the co-enzyme when Phe 34 side-chain is displaced (B) or mutated to Ala (C).	FIG
+21	27	hNaa60	protein	Structural basis for hNaa60 catalytic activity.	FIG
+4	17	Superposition	experimental_method	(A) Superposition of hNaa60 active site (cyan) on that of hNaa50 (pink, PDB 3TFY).	FIG
+21	27	hNaa60	protein	(A) Superposition of hNaa60 active site (cyan) on that of hNaa50 (pink, PDB 3TFY).	FIG
+28	39	active site	site	(A) Superposition of hNaa60 active site (cyan) on that of hNaa50 (pink, PDB 3TFY).	FIG
+58	64	hNaa50	protein	(A) Superposition of hNaa60 active site (cyan) on that of hNaa50 (pink, PDB 3TFY).	FIG
+19	59	catalytic and substrate-binding residues	site	Side-chains of key catalytic and substrate-binding residues are highlighted as sticks.	FIG
+4	12	malonate	chemical	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+29	49	hNaa60(1-242)/Ac-CoA	complex_assembly	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+50	59	structure	evidence	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+68	75	peptide	chemical	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+83	101	hNaa50/CoA/peptide	complex_assembly	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+102	111	structure	evidence	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+188	199	active site	site	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+203	209	hNaa60	protein	The malonate molecule in the hNaa60(1-242)/Ac-CoA structure and the peptide in the hNaa50/CoA/peptide structure are shown as purple and yellow sticks respectively. (B) A close view of the active site of hNaa60.	FIG
+9	15	Glu 37	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+17	23	Tyr 97	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+28	35	His 138	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+39	45	hNaa60	protein	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+81	87	Tyr 73	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+92	99	His 112	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+104	110	hNaa50	protein	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+171	177	Glu 24	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+179	185	His 72	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+190	197	His 111	residue_name_number	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+202	211	complexed	protein_state	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+219	226	hNaa10p	protein	Residues Glu 37, Tyr 97 and His 138 in hNaa60 (cyan) and corresponding residues (Tyr 73 and His 112) in hNaa50 (pink) as well as the side-chain of corresponding residues (Glu 24, His 72 and His 111) in complexed formed hNaa10p (warmpink) are highlighted as sticks.	FIG
+4	9	water	chemical	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+54	60	hNaa60	protein	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+65	71	hNaa50	protein	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+72	82	structures	evidence	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+164	172	malonate	chemical	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+223	243	hNaa60(1-242)/Ac-CoA	complex_assembly	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+244	253	structure	evidence	The water molecules participating in catalysis in the hNaa60 and hNaa50 structures are showed as green and red spheres, separately. (C) The interaction between the malonate molecule and surrounding residues observed in the hNaa60(1-242)/Ac-CoA structure.	FIG
+37	51	hydrogen bonds	bond_interaction	The yellow dotted lines indicate the hydrogen bonds. (D) A zoomed view of β3-β4 loop of hNaa60.	FIG
+74	84	β3-β4 loop	structure_element	The yellow dotted lines indicate the hydrogen bonds. (D) A zoomed view of β3-β4 loop of hNaa60.	FIG
+88	94	hNaa60	protein	The yellow dotted lines indicate the hydrogen bonds. (D) A zoomed view of β3-β4 loop of hNaa60.	FIG
+47	55	malonate	chemical	Key residues discussed in the text (cyan), the malonate (purple) and Ac-CoA (gray) are shown as sticks.	FIG
+69	75	Ac-CoA	chemical	Key residues discussed in the text (cyan), the malonate (purple) and Ac-CoA (gray) are shown as sticks.	FIG
+37	49	salt bridges	bond_interaction	The yellow dotted lines indicate the salt bridges.	FIG
+22	28	hNaa60	protein	Catalytic activity of hNaa60 and mutant proteins.	FIG
+33	39	mutant	protein_state	Catalytic activity of hNaa60 and mutant proteins.	FIG
+4	24	Catalytic efficiency	evidence	(A) Catalytic efficiency (shown as kcat/Km values) of hNaa60 (1-199) WT and mutants.	FIG
+35	39	kcat	evidence	(A) Catalytic efficiency (shown as kcat/Km values) of hNaa60 (1-199) WT and mutants.	FIG
+40	42	Km	evidence	(A) Catalytic efficiency (shown as kcat/Km values) of hNaa60 (1-199) WT and mutants.	FIG
+54	68	hNaa60 (1-199)	mutant	(A) Catalytic efficiency (shown as kcat/Km values) of hNaa60 (1-199) WT and mutants.	FIG
+69	71	WT	protein_state	(A) Catalytic efficiency (shown as kcat/Km values) of hNaa60 (1-199) WT and mutants.	FIG
+76	83	mutants	protein_state	(A) Catalytic efficiency (shown as kcat/Km values) of hNaa60 (1-199) WT and mutants.	FIG
+4	6	CD	experimental_method	(B) CD spectra of wild-type and mutant proteins from 250 nm to 190 nm.	FIG
+7	14	spectra	evidence	(B) CD spectra of wild-type and mutant proteins from 250 nm to 190 nm.	FIG
+18	27	wild-type	protein_state	(B) CD spectra of wild-type and mutant proteins from 250 nm to 190 nm.	FIG
+32	38	mutant	protein_state	(B) CD spectra of wild-type and mutant proteins from 250 nm to 190 nm.	FIG
+93	97	TCEP	chemical	The sample concentration was 4.5 μM in 20 mM Tris, pH 8.0, 150 mM NaCl, 1% glycerol and 1 mM TCEP at room temperature.	FIG
+0	41	Data collection and refinement statistics	evidence	Data collection and refinement statistics.	TABLE
+21	41	hNaa60(1-242)/Ac-CoA	complex_assembly	"Structure and PDB ID	hNaa60(1-242)/Ac-CoA 5HGZ	hNaa60(1-199)/CoA 5HH0	hNaa60(1-199)F34A/CoA 5HH1	 	Data collection*	 	 Space group	P212121	P21212	P21212	 	Cell dimensions	 	 a, b, c (Å)	53.3, 57.4, 68.8	67.8, 73.8, 43.2	66.7, 74.0, 43.5	 	 α,β,γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0	90.0, 90.0, 90.0	 	Resolution (Å)	50–1.38 (1.42–1.38)	50–1.60 (1.66–1.60)	50–1.80 (1.86–1.80)	 	Rp.i.m.(%)**	3.0 (34.4)	2.1 (32.5)	2.6 (47.8)	 	I/σ	21.5 (2.0)	31.8 (2.0)	28.0 (2.4)	 	Completeness (%)	99.8 (99.1)	99.6 (98.5)	99.9 (99.7)	 	Redundancy	6.9 (5.0)	6.9 (6.2)	6.3 (5.9)	 	Refinement	 	 Resolution (Å)	25.81–1.38	33.55–1.60	43.52–1.80	 	 No. reflections	43660	28588	20490	 	 Rwork/Rfree	0.182/0.192	0.181/0.184	0.189/0.209	 	No. atoms	 	 Protein	1717	1576	1566	 	 Ligand/ion	116	96	96	 	 Water	289	258	168	 	B-factors	 	 Protein	23.8	32.0	37.4	 	 Ligand/ion	22.2	34.6	43.7	 	 Water	35.1	46.4	49.1	 	R.m.s."	TABLE
+47	64	hNaa60(1-199)/CoA	complex_assembly	"Structure and PDB ID	hNaa60(1-242)/Ac-CoA 5HGZ	hNaa60(1-199)/CoA 5HH0	hNaa60(1-199)F34A/CoA 5HH1	 	Data collection*	 	 Space group	P212121	P21212	P21212	 	Cell dimensions	 	 a, b, c (Å)	53.3, 57.4, 68.8	67.8, 73.8, 43.2	66.7, 74.0, 43.5	 	 α,β,γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0	90.0, 90.0, 90.0	 	Resolution (Å)	50–1.38 (1.42–1.38)	50–1.60 (1.66–1.60)	50–1.80 (1.86–1.80)	 	Rp.i.m.(%)**	3.0 (34.4)	2.1 (32.5)	2.6 (47.8)	 	I/σ	21.5 (2.0)	31.8 (2.0)	28.0 (2.4)	 	Completeness (%)	99.8 (99.1)	99.6 (98.5)	99.9 (99.7)	 	Redundancy	6.9 (5.0)	6.9 (6.2)	6.3 (5.9)	 	Refinement	 	 Resolution (Å)	25.81–1.38	33.55–1.60	43.52–1.80	 	 No. reflections	43660	28588	20490	 	 Rwork/Rfree	0.182/0.192	0.181/0.184	0.189/0.209	 	No. atoms	 	 Protein	1717	1576	1566	 	 Ligand/ion	116	96	96	 	 Water	289	258	168	 	B-factors	 	 Protein	23.8	32.0	37.4	 	 Ligand/ion	22.2	34.6	43.7	 	 Water	35.1	46.4	49.1	 	R.m.s."	TABLE
+70	91	hNaa60(1-199)F34A/CoA	complex_assembly	"Structure and PDB ID	hNaa60(1-242)/Ac-CoA 5HGZ	hNaa60(1-199)/CoA 5HH0	hNaa60(1-199)F34A/CoA 5HH1	 	Data collection*	 	 Space group	P212121	P21212	P21212	 	Cell dimensions	 	 a, b, c (Å)	53.3, 57.4, 68.8	67.8, 73.8, 43.2	66.7, 74.0, 43.5	 	 α,β,γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0	90.0, 90.0, 90.0	 	Resolution (Å)	50–1.38 (1.42–1.38)	50–1.60 (1.66–1.60)	50–1.80 (1.86–1.80)	 	Rp.i.m.(%)**	3.0 (34.4)	2.1 (32.5)	2.6 (47.8)	 	I/σ	21.5 (2.0)	31.8 (2.0)	28.0 (2.4)	 	Completeness (%)	99.8 (99.1)	99.6 (98.5)	99.9 (99.7)	 	Redundancy	6.9 (5.0)	6.9 (6.2)	6.3 (5.9)	 	Refinement	 	 Resolution (Å)	25.81–1.38	33.55–1.60	43.52–1.80	 	 No. reflections	43660	28588	20490	 	 Rwork/Rfree	0.182/0.192	0.181/0.184	0.189/0.209	 	No. atoms	 	 Protein	1717	1576	1566	 	 Ligand/ion	116	96	96	 	 Water	289	258	168	 	B-factors	 	 Protein	23.8	32.0	37.4	 	 Ligand/ion	22.2	34.6	43.7	 	 Water	35.1	46.4	49.1	 	R.m.s."	TABLE
+780	785	Water	chemical	"Structure and PDB ID	hNaa60(1-242)/Ac-CoA 5HGZ	hNaa60(1-199)/CoA 5HH0	hNaa60(1-199)F34A/CoA 5HH1	 	Data collection*	 	 Space group	P212121	P21212	P21212	 	Cell dimensions	 	 a, b, c (Å)	53.3, 57.4, 68.8	67.8, 73.8, 43.2	66.7, 74.0, 43.5	 	 α,β,γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0	90.0, 90.0, 90.0	 	Resolution (Å)	50–1.38 (1.42–1.38)	50–1.60 (1.66–1.60)	50–1.80 (1.86–1.80)	 	Rp.i.m.(%)**	3.0 (34.4)	2.1 (32.5)	2.6 (47.8)	 	I/σ	21.5 (2.0)	31.8 (2.0)	28.0 (2.4)	 	Completeness (%)	99.8 (99.1)	99.6 (98.5)	99.9 (99.7)	 	Redundancy	6.9 (5.0)	6.9 (6.2)	6.3 (5.9)	 	Refinement	 	 Resolution (Å)	25.81–1.38	33.55–1.60	43.52–1.80	 	 No. reflections	43660	28588	20490	 	 Rwork/Rfree	0.182/0.192	0.181/0.184	0.189/0.209	 	No. atoms	 	 Protein	1717	1576	1566	 	 Ligand/ion	116	96	96	 	 Water	289	258	168	 	B-factors	 	 Protein	23.8	32.0	37.4	 	 Ligand/ion	22.2	34.6	43.7	 	 Water	35.1	46.4	49.1	 	R.m.s."	TABLE
+868	873	Water	chemical	"Structure and PDB ID	hNaa60(1-242)/Ac-CoA 5HGZ	hNaa60(1-199)/CoA 5HH0	hNaa60(1-199)F34A/CoA 5HH1	 	Data collection*	 	 Space group	P212121	P21212	P21212	 	Cell dimensions	 	 a, b, c (Å)	53.3, 57.4, 68.8	67.8, 73.8, 43.2	66.7, 74.0, 43.5	 	 α,β,γ (°)	90.0, 90.0, 90.0	90.0, 90.0, 90.0	90.0, 90.0, 90.0	 	Resolution (Å)	50–1.38 (1.42–1.38)	50–1.60 (1.66–1.60)	50–1.80 (1.86–1.80)	 	Rp.i.m.(%)**	3.0 (34.4)	2.1 (32.5)	2.6 (47.8)	 	I/σ	21.5 (2.0)	31.8 (2.0)	28.0 (2.4)	 	Completeness (%)	99.8 (99.1)	99.6 (98.5)	99.9 (99.7)	 	Redundancy	6.9 (5.0)	6.9 (6.2)	6.3 (5.9)	 	Refinement	 	 Resolution (Å)	25.81–1.38	33.55–1.60	43.52–1.80	 	 No. reflections	43660	28588	20490	 	 Rwork/Rfree	0.182/0.192	0.181/0.184	0.189/0.209	 	No. atoms	 	 Protein	1717	1576	1566	 	 Ligand/ion	116	96	96	 	 Water	289	258	168	 	B-factors	 	 Protein	23.8	32.0	37.4	 	 Ligand/ion	22.2	34.6	43.7	 	 Water	35.1	46.4	49.1	 	R.m.s."	TABLE
+4	11	crystal	evidence	One crystal was used for each data set.	TABLE
+36	44	R factor	evidence	**Rp.i.m., a redundancy-independent R factor was used to evaluate the diffraction data quality as was proposed by Evans.	TABLE
+70	86	diffraction data	evidence	**Rp.i.m., a redundancy-independent R factor was used to evaluate the diffraction data quality as was proposed by Evans.	TABLE