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+anno_start	anno_end	anno_text	entity_type	sentence	section
+0	18	Crystal Structures	evidence	Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana	TITLE
+31	44	Sugar Kinases	protein_type	Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana	TITLE
+50	82	Synechococcus Elongatus PCC 7942	species	Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana	TITLE
+87	107	Arabidopsis Thaliana	species	Crystal Structures of Putative Sugar Kinases from Synechococcus Elongatus PCC 7942 and Arabidopsis Thaliana	TITLE
+18	57	Synechococcus elongatus strain PCC 7942	species	The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana.	ABSTRACT
+77	89	sugar kinase	protein_type	The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana.	ABSTRACT
+91	96	SePSK	protein	The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana.	ABSTRACT
+145	162	xylulose kinase-1	protein	The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana.	ABSTRACT
+164	170	AtXK-1	protein	The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana.	ABSTRACT
+177	197	Arabidopsis thaliana	species	The genome of the Synechococcus elongatus strain PCC 7942 encodes a putative sugar kinase (SePSK), which shares 44.9% sequence identity with the xylulose kinase-1 (AtXK-1) from Arabidopsis thaliana.	ABSTRACT
+0	18	Sequence alignment	experimental_method	Sequence alignment suggests that both kinases belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	ABSTRACT
+38	45	kinases	protein_type	Sequence alignment suggests that both kinases belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	ABSTRACT
+60	98	ribulokinase-like carbohydrate kinases	protein_type	Sequence alignment suggests that both kinases belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	ABSTRACT
+116	148	FGGY family carbohydrate kinases	protein_type	Sequence alignment suggests that both kinases belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	ABSTRACT
+8	14	solved	experimental_method	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+19	29	structures	evidence	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+33	38	SePSK	protein	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+43	49	AtXK-1	protein	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+64	67	apo	protein_state	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+78	93	in complex with	protein_state	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+94	104	nucleotide	chemical	Here we solved the structures of SePSK and AtXK-1 in both their apo forms and in complex with nucleotide substrates.	ABSTRACT
+73	80	kinases	protein_type	The two kinases exhibit nearly identical overall architecture, with both kinases possessing ATP hydrolysis activity in the absence of substrates.	ABSTRACT
+92	95	ATP	chemical	The two kinases exhibit nearly identical overall architecture, with both kinases possessing ATP hydrolysis activity in the absence of substrates.	ABSTRACT
+123	144	absence of substrates	protein_state	The two kinases exhibit nearly identical overall architecture, with both kinases possessing ATP hydrolysis activity in the absence of substrates.	ABSTRACT
+17	33	enzymatic assays	experimental_method	In addition, our enzymatic assays suggested that SePSK has the capability to phosphorylate D-ribulose.	ABSTRACT
+49	54	SePSK	protein	In addition, our enzymatic assays suggested that SePSK has the capability to phosphorylate D-ribulose.	ABSTRACT
+91	101	D-ribulose	chemical	In addition, our enzymatic assays suggested that SePSK has the capability to phosphorylate D-ribulose.	ABSTRACT
+50	55	SePSK	protein	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+60	66	solved	experimental_method	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+71	80	structure	evidence	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+84	89	SePSK	protein	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+90	105	in complex with	protein_state	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+106	116	D-ribulose	chemical	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+141	166	substrate binding pockets	site	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+170	175	SePSK	protein	In order to understand the catalytic mechanism of SePSK, we solved the structure of SePSK in complex with D-ribulose and found two potential substrate binding pockets in SePSK.	ABSTRACT
+6	36	mutation and activity analysis	experimental_method	Using mutation and activity analysis, we further verified the key residues important for its catalytic activity.	ABSTRACT
+14	35	structural comparison	experimental_method	Moreover, our structural comparison with other family members suggests that there are major conformational changes in SePSK upon substrate binding, facilitating the catalytic process.	ABSTRACT
+118	123	SePSK	protein	Moreover, our structural comparison with other family members suggests that there are major conformational changes in SePSK upon substrate binding, facilitating the catalytic process.	ABSTRACT
+169	174	SePSK	protein	Together, these results provide important information for a more detailed understanding of the cofactor and substrate binding mode as well as the catalytic mechanism of SePSK, and possible similarities with its plant homologue AtXK-1.	ABSTRACT
+211	216	plant	taxonomy_domain	Together, these results provide important information for a more detailed understanding of the cofactor and substrate binding mode as well as the catalytic mechanism of SePSK, and possible similarities with its plant homologue AtXK-1.	ABSTRACT
+227	233	AtXK-1	protein	Together, these results provide important information for a more detailed understanding of the cofactor and substrate binding mode as well as the catalytic mechanism of SePSK, and possible similarities with its plant homologue AtXK-1.	ABSTRACT
+0	13	Carbohydrates	chemical	Carbohydrates are essential cellular compounds involved in the metabolic processes present in all organisms.	INTRO
+0	15	Phosphorylation	ptm	Phosphorylation is one of the various pivotal modifications of carbohydrates, and is catalyzed by specific sugar kinases.	INTRO
+63	76	carbohydrates	chemical	Phosphorylation is one of the various pivotal modifications of carbohydrates, and is catalyzed by specific sugar kinases.	INTRO
+107	120	sugar kinases	protein_type	Phosphorylation is one of the various pivotal modifications of carbohydrates, and is catalyzed by specific sugar kinases.	INTRO
+6	13	kinases	protein_type	These kinases exhibit considerable differences in their folding pattern and substrate specificity.	INTRO
+9	26	sequence analysis	experimental_method	Based on sequence analysis, they can be divided into four families, namely HSP 70_NBD family, FGGY family, Mer_B like family and Parm_like family.	INTRO
+75	92	HSP 70_NBD family	protein_type	Based on sequence analysis, they can be divided into four families, namely HSP 70_NBD family, FGGY family, Mer_B like family and Parm_like family.	INTRO
+94	105	FGGY family	protein_type	Based on sequence analysis, they can be divided into four families, namely HSP 70_NBD family, FGGY family, Mer_B like family and Parm_like family.	INTRO
+107	124	Mer_B like family	protein_type	Based on sequence analysis, they can be divided into four families, namely HSP 70_NBD family, FGGY family, Mer_B like family and Parm_like family.	INTRO
+129	145	Parm_like family	protein_type	Based on sequence analysis, they can be divided into four families, namely HSP 70_NBD family, FGGY family, Mer_B like family and Parm_like family.	INTRO
+4	36	FGGY family carbohydrate kinases	protein_type	The FGGY family carbohydrate kinases contain different types of sugar kinases, all of which possess different catalytic substrates with preferences for short-chained sugar substrates, ranging from triose to heptose.	INTRO
+64	77	sugar kinases	protein_type	The FGGY family carbohydrate kinases contain different types of sugar kinases, all of which possess different catalytic substrates with preferences for short-chained sugar substrates, ranging from triose to heptose.	INTRO
+166	171	sugar	chemical	The FGGY family carbohydrate kinases contain different types of sugar kinases, all of which possess different catalytic substrates with preferences for short-chained sugar substrates, ranging from triose to heptose.	INTRO
+197	203	triose	chemical	The FGGY family carbohydrate kinases contain different types of sugar kinases, all of which possess different catalytic substrates with preferences for short-chained sugar substrates, ranging from triose to heptose.	INTRO
+207	214	heptose	chemical	The FGGY family carbohydrate kinases contain different types of sugar kinases, all of which possess different catalytic substrates with preferences for short-chained sugar substrates, ranging from triose to heptose.	INTRO
+6	11	sugar	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+31	41	L-ribulose	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+43	53	erythritol	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+55	65	L-fuculose	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+67	77	D-glycerol	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+79	90	D-gluconate	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+92	102	L-xylulose	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+104	114	D-ribulose	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+116	128	L-rhamnulose	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+133	143	D-xylulose	chemical	These sugar substrates include L-ribulose, erythritol, L-fuculose, D-glycerol, D-gluconate, L-xylulose, D-ribulose, L-rhamnulose and D-xylulose.	INTRO
+0	10	Structures	evidence	Structures reported in the Protein Data Bank of the FGGY family carbohydrate kinases exhibit a similar overall architecture containing two protein domains, one of which is responsible for the binding of substrate, while the second is used for binding cofactor ATP.	INTRO
+52	84	FGGY family carbohydrate kinases	protein_type	Structures reported in the Protein Data Bank of the FGGY family carbohydrate kinases exhibit a similar overall architecture containing two protein domains, one of which is responsible for the binding of substrate, while the second is used for binding cofactor ATP.	INTRO
+260	263	ATP	chemical	Structures reported in the Protein Data Bank of the FGGY family carbohydrate kinases exhibit a similar overall architecture containing two protein domains, one of which is responsible for the binding of substrate, while the second is used for binding cofactor ATP.	INTRO
+10	25	binding pockets	site	While the binding pockets for substrates are at the same position, each FGGY family carbohydrate kinases uses different substrate-binding residues, resulting in high substrate specificity.	INTRO
+72	104	FGGY family carbohydrate kinases	protein_type	While the binding pockets for substrates are at the same position, each FGGY family carbohydrate kinases uses different substrate-binding residues, resulting in high substrate specificity.	INTRO
+120	146	substrate-binding residues	site	While the binding pockets for substrates are at the same position, each FGGY family carbohydrate kinases uses different substrate-binding residues, resulting in high substrate specificity.	INTRO
+0	15	Synpcc7942_2462	gene	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+25	38	cyanobacteria	taxonomy_domain	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+39	71	Synechococcus elongatus PCC 7942	species	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+91	103	sugar kinase	protein_type	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+105	110	SePSK	protein	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+122	128	kinase	protein_type	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+138	141	426	residue_range	Synpcc7942_2462 from the cyanobacteria Synechococcus elongatus PCC 7942 encodes a putative sugar kinase (SePSK), and this kinase contains 426 amino acids.	INTRO
+4	13	At2g21370	gene	The At2g21370 gene product from Arabidopsis thaliana, xylulose kinase-1 (AtXK-1), whose mature form contains 436 amino acids, is located in the chloroplast (ChloroP 1.1 Server).	INTRO
+32	52	Arabidopsis thaliana	species	The At2g21370 gene product from Arabidopsis thaliana, xylulose kinase-1 (AtXK-1), whose mature form contains 436 amino acids, is located in the chloroplast (ChloroP 1.1 Server).	INTRO
+54	71	xylulose kinase-1	protein	The At2g21370 gene product from Arabidopsis thaliana, xylulose kinase-1 (AtXK-1), whose mature form contains 436 amino acids, is located in the chloroplast (ChloroP 1.1 Server).	INTRO
+73	79	AtXK-1	protein	The At2g21370 gene product from Arabidopsis thaliana, xylulose kinase-1 (AtXK-1), whose mature form contains 436 amino acids, is located in the chloroplast (ChloroP 1.1 Server).	INTRO
+88	99	mature form	protein_state	The At2g21370 gene product from Arabidopsis thaliana, xylulose kinase-1 (AtXK-1), whose mature form contains 436 amino acids, is located in the chloroplast (ChloroP 1.1 Server).	INTRO
+109	112	436	residue_range	The At2g21370 gene product from Arabidopsis thaliana, xylulose kinase-1 (AtXK-1), whose mature form contains 436 amino acids, is located in the chloroplast (ChloroP 1.1 Server).	INTRO
+0	5	SePSK	protein	SePSK and AtXK-1 display a sequence identity of 44.9%, and belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	INTRO
+10	16	AtXK-1	protein	SePSK and AtXK-1 display a sequence identity of 44.9%, and belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	INTRO
+73	111	ribulokinase-like carbohydrate kinases	protein_type	SePSK and AtXK-1 display a sequence identity of 44.9%, and belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	INTRO
+129	161	FGGY family carbohydrate kinases	protein_type	SePSK and AtXK-1 display a sequence identity of 44.9%, and belong to the ribulokinase-like carbohydrate kinases, a sub-family of FGGY family carbohydrate kinases.	INTRO
+51	66	phosphorylation	ptm	Members of this sub-family are responsible for the phosphorylation of sugars similar to L-ribulose and D-ribulose.	INTRO
+70	76	sugars	chemical	Members of this sub-family are responsible for the phosphorylation of sugars similar to L-ribulose and D-ribulose.	INTRO
+88	98	L-ribulose	chemical	Members of this sub-family are responsible for the phosphorylation of sugars similar to L-ribulose and D-ribulose.	INTRO
+103	113	D-ribulose	chemical	Members of this sub-family are responsible for the phosphorylation of sugars similar to L-ribulose and D-ribulose.	INTRO
+46	84	ribulokinase-like carbohydrate kinases	protein_type	The sequence and the substrate specificity of ribulokinase-like carbohydrate kinases are different, but they share the common folding feature with two domains.	INTRO
+0	8	Domain I	structure_element	Domain I exhibits a ribonuclease H-like folding pattern, and is responsible for the substrate binding, while domain II possesses an actin-like ATPase domain that binds cofactor ATP.	INTRO
+20	55	ribonuclease H-like folding pattern	structure_element	Domain I exhibits a ribonuclease H-like folding pattern, and is responsible for the substrate binding, while domain II possesses an actin-like ATPase domain that binds cofactor ATP.	INTRO
+109	118	domain II	structure_element	Domain I exhibits a ribonuclease H-like folding pattern, and is responsible for the substrate binding, while domain II possesses an actin-like ATPase domain that binds cofactor ATP.	INTRO
+132	156	actin-like ATPase domain	structure_element	Domain I exhibits a ribonuclease H-like folding pattern, and is responsible for the substrate binding, while domain II possesses an actin-like ATPase domain that binds cofactor ATP.	INTRO
+177	180	ATP	chemical	Domain I exhibits a ribonuclease H-like folding pattern, and is responsible for the substrate binding, while domain II possesses an actin-like ATPase domain that binds cofactor ATP.	INTRO
+13	29	xylulose kinases	protein_type	Two possible xylulose kinases (xylulose kinase-1: XK-1 and xylulose kinase-2: XK-2) from Arabidopsis thaliana were previously proposed.	INTRO
+31	48	xylulose kinase-1	protein	Two possible xylulose kinases (xylulose kinase-1: XK-1 and xylulose kinase-2: XK-2) from Arabidopsis thaliana were previously proposed.	INTRO
+50	54	XK-1	protein	Two possible xylulose kinases (xylulose kinase-1: XK-1 and xylulose kinase-2: XK-2) from Arabidopsis thaliana were previously proposed.	INTRO
+59	76	xylulose kinase-2	protein	Two possible xylulose kinases (xylulose kinase-1: XK-1 and xylulose kinase-2: XK-2) from Arabidopsis thaliana were previously proposed.	INTRO
+78	82	XK-2	protein	Two possible xylulose kinases (xylulose kinase-1: XK-1 and xylulose kinase-2: XK-2) from Arabidopsis thaliana were previously proposed.	INTRO
+89	109	Arabidopsis thaliana	species	Two possible xylulose kinases (xylulose kinase-1: XK-1 and xylulose kinase-2: XK-2) from Arabidopsis thaliana were previously proposed.	INTRO
+18	22	XK-2	protein	It was shown that XK-2 (At5g49650) located in the cytosol is indeed xylulose kinase.	INTRO
+24	33	At5g49650	gene	It was shown that XK-2 (At5g49650) located in the cytosol is indeed xylulose kinase.	INTRO
+68	83	xylulose kinase	protein_type	It was shown that XK-2 (At5g49650) located in the cytosol is indeed xylulose kinase.	INTRO
+25	29	XK-1	protein	However, the function of XK-1 (At2g21370) inside the chloroplast stroma has remained unknown.	INTRO
+31	40	At2g21370	gene	However, the function of XK-1 (At2g21370) inside the chloroplast stroma has remained unknown.	INTRO
+0	5	SePSK	protein	SePSK from Synechococcus elongatus strain PCC 7942 is the homolog of AtXK-1, though its physiological function and substrates remain unclear.	INTRO
+11	50	Synechococcus elongatus strain PCC 7942	species	SePSK from Synechococcus elongatus strain PCC 7942 is the homolog of AtXK-1, though its physiological function and substrates remain unclear.	INTRO
+69	75	AtXK-1	protein	SePSK from Synechococcus elongatus strain PCC 7942 is the homolog of AtXK-1, though its physiological function and substrates remain unclear.	INTRO
+104	122	crystal structures	evidence	In order to obtain functional and structural information about these two proteins, here we reported the crystal structures of SePSK and AtXK-1.	INTRO
+126	131	SePSK	protein	In order to obtain functional and structural information about these two proteins, here we reported the crystal structures of SePSK and AtXK-1.	INTRO
+136	142	AtXK-1	protein	In order to obtain functional and structural information about these two proteins, here we reported the crystal structures of SePSK and AtXK-1.	INTRO
+63	68	SePSK	protein	Our findings provide new details of the catalytic mechanism of SePSK and lay the foundation for future studies into its homologs in eukaryotes.	INTRO
+132	142	eukaryotes	taxonomy_domain	Our findings provide new details of the catalytic mechanism of SePSK and lay the foundation for future studies into its homologs in eukaryotes.	INTRO
+8	18	structures	evidence	Overall structures of apo-SePSK and apo-AtXK-1	RESULTS
+22	25	apo	protein_state	Overall structures of apo-SePSK and apo-AtXK-1	RESULTS
+26	31	SePSK	protein	Overall structures of apo-SePSK and apo-AtXK-1	RESULTS
+36	39	apo	protein_state	Overall structures of apo-SePSK and apo-AtXK-1	RESULTS
+40	46	AtXK-1	protein	Overall structures of apo-SePSK and apo-AtXK-1	RESULTS
+25	30	SePSK	protein	The attempt to solve the SePSK structure by molecular replacement method failed with ribulokinase from Bacillus halodurans (PDB code: 3QDK, 15.7% sequence identity) as an initial model.	RESULTS
+31	40	structure	evidence	The attempt to solve the SePSK structure by molecular replacement method failed with ribulokinase from Bacillus halodurans (PDB code: 3QDK, 15.7% sequence identity) as an initial model.	RESULTS
+44	72	molecular replacement method	experimental_method	The attempt to solve the SePSK structure by molecular replacement method failed with ribulokinase from Bacillus halodurans (PDB code: 3QDK, 15.7% sequence identity) as an initial model.	RESULTS
+85	97	ribulokinase	protein	The attempt to solve the SePSK structure by molecular replacement method failed with ribulokinase from Bacillus halodurans (PDB code: 3QDK, 15.7% sequence identity) as an initial model.	RESULTS
+103	122	Bacillus halodurans	species	The attempt to solve the SePSK structure by molecular replacement method failed with ribulokinase from Bacillus halodurans (PDB code: 3QDK, 15.7% sequence identity) as an initial model.	RESULTS
+18	76	single isomorphous replacement anomalous scattering method	experimental_method	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+78	83	SIRAS	experimental_method	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+116	119	apo	protein_state	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+120	125	SePSK	protein	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+126	135	structure	evidence	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+180	183	apo	protein_state	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+184	189	SePSK	protein	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+190	199	structure	evidence	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+212	239	molecular replacement model	experimental_method	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+259	269	structures	evidence	We therefore used single isomorphous replacement anomalous scattering method (SIRAS) for successful solution of the apo-SePSK structure at a resolution of 2.3 Å. Subsequently, the apo-SePSK structure was used as molecular replacement model to solve all other structures identified in this study.	RESULTS
+4	23	structural analysis	experimental_method	Our structural analysis showed that apo-SePSK consists of one SePSK protein molecule in an asymmetric unit.	RESULTS
+36	39	apo	protein_state	Our structural analysis showed that apo-SePSK consists of one SePSK protein molecule in an asymmetric unit.	RESULTS
+40	45	SePSK	protein	Our structural analysis showed that apo-SePSK consists of one SePSK protein molecule in an asymmetric unit.	RESULTS
+62	67	SePSK	protein	Our structural analysis showed that apo-SePSK consists of one SePSK protein molecule in an asymmetric unit.	RESULTS
+41	45	Val2	residue_name_number	The amino-acid residues were traced from Val2 to His419, except for the Met1 residue and the seven residues at the C-termini.	RESULTS
+49	55	His419	residue_name_number	The amino-acid residues were traced from Val2 to His419, except for the Met1 residue and the seven residues at the C-termini.	RESULTS
+72	76	Met1	residue_name_number	The amino-acid residues were traced from Val2 to His419, except for the Met1 residue and the seven residues at the C-termini.	RESULTS
+0	3	Apo	protein_state	Apo-SePSK contains two domains referred to further on as domain I and domain II (Fig 1A).	RESULTS
+4	9	SePSK	protein	Apo-SePSK contains two domains referred to further on as domain I and domain II (Fig 1A).	RESULTS
+57	65	domain I	structure_element	Apo-SePSK contains two domains referred to further on as domain I and domain II (Fig 1A).	RESULTS
+70	79	domain II	structure_element	Apo-SePSK contains two domains referred to further on as domain I and domain II (Fig 1A).	RESULTS
+0	8	Domain I	structure_element	Domain I consists of non-contiguous portions of the polypeptide chains (aa.	RESULTS
+0	5	2–228	residue_range	2–228 and aa.	RESULTS
+0	7	402–419	residue_range	402–419), exhibiting 11 α-helices and 11 β-sheets.	RESULTS
+24	33	α-helices	structure_element	402–419), exhibiting 11 α-helices and 11 β-sheets.	RESULTS
+41	49	β-sheets	structure_element	402–419), exhibiting 11 α-helices and 11 β-sheets.	RESULTS
+37	39	α4	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+40	42	α5	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+43	46	α11	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+47	50	α18	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+52	54	β3	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+55	57	β2	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+58	60	β1	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+61	63	β6	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+64	67	β19	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+68	71	β20	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+72	75	β17	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+80	83	α21	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+84	87	α32	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+123	125	A1	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+127	129	B1	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+134	136	A2	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+153	164	core region	structure_element	Among all these structural elements, α4/α5/α11/α18, β3/β2/β1/β6/β19/β20/β17 and α21/α32 form three patches, referred to as A1, B1 and A2, exhibiting the core region.	RESULTS
+18	26	β-sheets	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+28	30	β7	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+32	35	β10	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+37	40	β12	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+45	48	β16	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+59	68	α-helices	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+70	72	α8	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+74	76	α9	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+78	81	α13	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+83	86	α14	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+91	94	α15	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+123	134	core region	structure_element	In addition, four β-sheets (β7, β10, β12 and β16) and five α-helices (α8, α9, α13, α14 and α15) flank the left side of the core region.	RESULTS
+0	9	Domain II	structure_element	Domain II is comprised of aa.	RESULTS
+0	7	229–401	residue_range	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+28	30	B2	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+32	35	β31	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+36	39	β29	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+40	43	β22	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+44	47	β23	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+48	51	β25	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+52	55	β24	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+61	63	A3	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+65	68	α26	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+69	72	α27	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+73	76	α28	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+77	80	α30	structure_element	229–401 and classified into B2 (β31/β29/β22/β23/β25/β24) and A3 (α26/α27/α28/α30) (Fig 1A and S1 Fig).	RESULTS
+7	12	SePSK	protein	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+13	22	structure	evidence	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+24	26	B1	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+31	33	B2	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+52	54	A1	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+56	58	A2	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+63	65	A3	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+81	90	structure	evidence	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+101	103	A1	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+104	106	B1	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+107	109	A2	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+110	112	B2	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+113	115	A3	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+117	118	α	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+119	120	β	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+121	122	α	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+123	124	β	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+125	126	α	structure_element	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+186	218	FGGY family carbohydrate kinases	protein_type	In the SePSK structure, B1 and B2 are sandwiched by A1, A2 and A3, and the whole structure shows the A1/B1/A2/B2/A3 (α/β/α/β/α) folding pattern, which is in common with other members of FGGY family carbohydrate kinases (S2 Fig).	RESULTS
+23	28	SePSK	protein	The overall folding of SePSK resembles a clip, with A2 of domain I acting as a hinge region.	RESULTS
+52	54	A2	structure_element	The overall folding of SePSK resembles a clip, with A2 of domain I acting as a hinge region.	RESULTS
+58	66	domain I	structure_element	The overall folding of SePSK resembles a clip, with A2 of domain I acting as a hinge region.	RESULTS
+79	91	hinge region	structure_element	The overall folding of SePSK resembles a clip, with A2 of domain I acting as a hinge region.	RESULTS
+8	18	structures	evidence	Overall structures of SePSK and AtXK-1.	FIG
+22	27	SePSK	protein	Overall structures of SePSK and AtXK-1.	FIG
+32	38	AtXK-1	protein	Overall structures of SePSK and AtXK-1.	FIG
+22	31	structure	evidence	(A) Three-dimensional structure of apo-SePSK.	FIG
+35	38	apo	protein_state	(A) Three-dimensional structure of apo-SePSK.	FIG
+39	44	SePSK	protein	(A) Three-dimensional structure of apo-SePSK.	FIG
+49	56	α-helix	structure_element	The secondary structural elements are indicated (α-helix: cyan, β-sheet: yellow).	FIG
+64	71	β-sheet	structure_element	The secondary structural elements are indicated (α-helix: cyan, β-sheet: yellow).	FIG
+22	31	structure	evidence	(B) Three-dimensional structure of apo-AtXK-1.	FIG
+35	38	apo	protein_state	(B) Three-dimensional structure of apo-AtXK-1.	FIG
+39	45	AtXK-1	protein	(B) Three-dimensional structure of apo-AtXK-1.	FIG
+49	56	α-helix	structure_element	The secondary structural elements are indicated (α-helix: green, β-sheet: wheat).	FIG
+65	72	β-sheet	structure_element	The secondary structural elements are indicated (α-helix: green, β-sheet: wheat).	FIG
+0	3	Apo	protein_state	Apo-AtXK-1 exhibits a folding pattern similar to that of SePSK in line with their high sequence identity (Fig 1B and S1 Fig).	RESULTS
+4	10	AtXK-1	protein	Apo-AtXK-1 exhibits a folding pattern similar to that of SePSK in line with their high sequence identity (Fig 1B and S1 Fig).	RESULTS
+57	62	SePSK	protein	Apo-AtXK-1 exhibits a folding pattern similar to that of SePSK in line with their high sequence identity (Fig 1B and S1 Fig).	RESULTS
+9	22	superposition	experimental_method	However, superposition of structures of AtXK-1 and SePSK shows some differences, especially at the loop regions.	RESULTS
+26	36	structures	evidence	However, superposition of structures of AtXK-1 and SePSK shows some differences, especially at the loop regions.	RESULTS
+40	46	AtXK-1	protein	However, superposition of structures of AtXK-1 and SePSK shows some differences, especially at the loop regions.	RESULTS
+51	56	SePSK	protein	However, superposition of structures of AtXK-1 and SePSK shows some differences, especially at the loop regions.	RESULTS
+99	111	loop regions	structure_element	However, superposition of structures of AtXK-1 and SePSK shows some differences, especially at the loop regions.	RESULTS
+42	47	loop3	structure_element	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+56	58	β3	structure_element	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+63	65	α4	structure_element	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+97	103	AtXK-1	protein	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+104	113	structure	evidence	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+128	133	SePSK	protein	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+134	143	structure	evidence	A considerable difference is found in the loop3 linking β3 and α4, which is stretched out in the AtXK-1 structure, while in the SePSK structure, it is bent back towards the inner part.	RESULTS
+45	55	structures	evidence	The corresponding residues between these two structures (SePSK-Lys35 and AtXK-1-Lys48) have a distance of 15.4 Å (S3 Fig).	RESULTS
+57	62	SePSK	protein	The corresponding residues between these two structures (SePSK-Lys35 and AtXK-1-Lys48) have a distance of 15.4 Å (S3 Fig).	RESULTS
+63	68	Lys35	residue_name_number	The corresponding residues between these two structures (SePSK-Lys35 and AtXK-1-Lys48) have a distance of 15.4 Å (S3 Fig).	RESULTS
+73	79	AtXK-1	protein	The corresponding residues between these two structures (SePSK-Lys35 and AtXK-1-Lys48) have a distance of 15.4 Å (S3 Fig).	RESULTS
+80	85	Lys48	residue_name_number	The corresponding residues between these two structures (SePSK-Lys35 and AtXK-1-Lys48) have a distance of 15.4 Å (S3 Fig).	RESULTS
+0	15	Activity assays	experimental_method	Activity assays of SePSK and AtXK-1	RESULTS
+19	24	SePSK	protein	Activity assays of SePSK and AtXK-1	RESULTS
+29	35	AtXK-1	protein	Activity assays of SePSK and AtXK-1	RESULTS
+71	92	structural comparison	experimental_method	In order to understand the function of these two kinases, we performed structural comparison using Dali server.	RESULTS
+99	110	Dali server	experimental_method	In order to understand the function of these two kinases, we performed structural comparison using Dali server.	RESULTS
+4	14	structures	evidence	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+39	44	SePSK	protein	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+49	64	xylulose kinase	protein_type	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+66	81	glycerol kinase	protein_type	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+86	101	ribulose kinase	protein_type	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+117	122	SePSK	protein	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+127	133	AtXK-1	protein	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+168	175	kinases	protein_type	The structures most closely related to SePSK are xylulose kinase, glycerol kinase and ribulose kinase, implying that SePSK and AtXK-1 might function similarly to these kinases.	RESULTS
+47	50	ATP	chemical	We first tested whether both enzymes possessed ATP hydrolysis activity in the absence of substrates.	RESULTS
+78	88	absence of	protein_state	We first tested whether both enzymes possessed ATP hydrolysis activity in the absence of substrates.	RESULTS
+25	30	SePSK	protein	As shown in Fig 2A, both SePSK and AtXK-1 exhibited ATP hydrolysis activity.	RESULTS
+35	41	AtXK-1	protein	As shown in Fig 2A, both SePSK and AtXK-1 exhibited ATP hydrolysis activity.	RESULTS
+52	55	ATP	chemical	As shown in Fig 2A, both SePSK and AtXK-1 exhibited ATP hydrolysis activity.	RESULTS
+65	80	xylulose kinase	protein_type	This finding is in agreement with a previous result showing that xylulose kinase (PDB code: 2ITM) possessed ATP hydrolysis activity without adding substrate.	RESULTS
+108	111	ATP	chemical	This finding is in agreement with a previous result showing that xylulose kinase (PDB code: 2ITM) possessed ATP hydrolysis activity without adding substrate.	RESULTS
+44	49	SePSK	protein	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+54	60	AtXK-1	protein	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+104	114	D-ribulose	chemical	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+116	126	L-ribulose	chemical	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+128	138	D-xylulose	chemical	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+140	150	L-xylulose	chemical	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+155	163	Glycerol	chemical	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+178	203	enzymatic activity assays	experimental_method	To further identify the actual substrate of SePSK and AtXK-1, five different sugar molecules, including D-ribulose, L-ribulose, D-xylulose, L-xylulose and Glycerol, were used in enzymatic activity assays.	RESULTS
+24	27	ATP	chemical	As shown in Fig 2B, the ATP hydrolysis activity of SePSK greatly increased upon adding D-ribulose than adding other potential substrates, suggesting that it has D-ribulose kinase activity.	RESULTS
+51	56	SePSK	protein	As shown in Fig 2B, the ATP hydrolysis activity of SePSK greatly increased upon adding D-ribulose than adding other potential substrates, suggesting that it has D-ribulose kinase activity.	RESULTS
+87	97	D-ribulose	chemical	As shown in Fig 2B, the ATP hydrolysis activity of SePSK greatly increased upon adding D-ribulose than adding other potential substrates, suggesting that it has D-ribulose kinase activity.	RESULTS
+161	178	D-ribulose kinase	protein_type	As shown in Fig 2B, the ATP hydrolysis activity of SePSK greatly increased upon adding D-ribulose than adding other potential substrates, suggesting that it has D-ribulose kinase activity.	RESULTS
+35	38	ATP	chemical	In contrary, limited increasing of ATP hydrolysis activity was detected for AtXK-1 upon addition of D-ribulose (Fig 2C), despite its structural similarity with SePSK.	RESULTS
+76	82	AtXK-1	protein	In contrary, limited increasing of ATP hydrolysis activity was detected for AtXK-1 upon addition of D-ribulose (Fig 2C), despite its structural similarity with SePSK.	RESULTS
+100	110	D-ribulose	chemical	In contrary, limited increasing of ATP hydrolysis activity was detected for AtXK-1 upon addition of D-ribulose (Fig 2C), despite its structural similarity with SePSK.	RESULTS
+160	165	SePSK	protein	In contrary, limited increasing of ATP hydrolysis activity was detected for AtXK-1 upon addition of D-ribulose (Fig 2C), despite its structural similarity with SePSK.	RESULTS
+4	29	enzymatic activity assays	experimental_method	The enzymatic activity assays of SePSK and AtXK-1.	FIG
+33	38	SePSK	protein	The enzymatic activity assays of SePSK and AtXK-1.	FIG
+43	49	AtXK-1	protein	The enzymatic activity assays of SePSK and AtXK-1.	FIG
+8	11	ATP	chemical	(A) The ATP hydrolysis activity of SePSK and AtXK-1.	FIG
+35	40	SePSK	protein	(A) The ATP hydrolysis activity of SePSK and AtXK-1.	FIG
+45	51	AtXK-1	protein	(A) The ATP hydrolysis activity of SePSK and AtXK-1.	FIG
+5	10	SePSK	protein	Both SePSK and AtXK-1 showed ATP hydrolysis activity in the absence of substrate.	FIG
+15	21	AtXK-1	protein	Both SePSK and AtXK-1 showed ATP hydrolysis activity in the absence of substrate.	FIG
+29	32	ATP	chemical	Both SePSK and AtXK-1 showed ATP hydrolysis activity in the absence of substrate.	FIG
+60	70	absence of	protein_state	Both SePSK and AtXK-1 showed ATP hydrolysis activity in the absence of substrate.	FIG
+10	13	ATP	chemical	While the ATP hydrolysis activity of SePSK greatly increases upon addition of D-ribulose (DR).	FIG
+37	42	SePSK	protein	While the ATP hydrolysis activity of SePSK greatly increases upon addition of D-ribulose (DR).	FIG
+78	88	D-ribulose	chemical	While the ATP hydrolysis activity of SePSK greatly increases upon addition of D-ribulose (DR).	FIG
+90	92	DR	chemical	While the ATP hydrolysis activity of SePSK greatly increases upon addition of D-ribulose (DR).	FIG
+8	11	ATP	chemical	(B) The ATP hydrolysis activity of SePSK with addition of five different substrates.	FIG
+35	40	SePSK	protein	(B) The ATP hydrolysis activity of SePSK with addition of five different substrates.	FIG
+19	21	DR	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+23	33	D-ribulose	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+36	38	LR	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+40	50	L-ribulose	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+53	55	DX	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+57	67	D-xylulose	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+70	72	LX	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+74	84	L-xylulose	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+90	93	GLY	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+95	103	Glycerol	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+114	117	ATP	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+141	146	SePSK	protein	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+151	157	AtXK-1	protein	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+174	184	D-ribulose	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+194	197	ATP	chemical	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+221	230	wild-type	protein_state	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+232	234	WT	protein_state	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+263	268	SePSK	protein	The substrates are DR (D-ribulose), LR (L-ribulose), DX (D-xylulose), LX (L-xylulose) and GLY (Glycerol). (C) The ATP hydrolysis activity of SePSK and AtXK-1 with or without D-ribulose. (D) The ATP hydrolysis activity of wild-type (WT) and single-site mutants of SePSK.	FIG
+29	34	SePSK	protein	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+39	42	D8A	mutant	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+43	48	SePSK	protein	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+50	54	T11A	mutant	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+55	60	SePSK	protein	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+65	70	D221A	mutant	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+71	76	SePSK	protein	Three single-site mutants of SePSK are D8A-SePSK, T11A-SePSK and D221A-SePSK.	FIG
+4	7	ATP	chemical	The ATP hydrolysis activity measured via luminescent ADP-Glo assay (Promega).	FIG
+41	66	luminescent ADP-Glo assay	experimental_method	The ATP hydrolysis activity measured via luminescent ADP-Glo assay (Promega).	FIG
+41	46	SePSK	protein	To understand the catalytic mechanism of SePSK, we performed structural comparisons among xylulose kinase, glycerol kinase, ribulose kinase and SePSK.	RESULTS
+61	83	structural comparisons	experimental_method	To understand the catalytic mechanism of SePSK, we performed structural comparisons among xylulose kinase, glycerol kinase, ribulose kinase and SePSK.	RESULTS
+90	105	xylulose kinase	protein_type	To understand the catalytic mechanism of SePSK, we performed structural comparisons among xylulose kinase, glycerol kinase, ribulose kinase and SePSK.	RESULTS
+107	122	glycerol kinase	protein_type	To understand the catalytic mechanism of SePSK, we performed structural comparisons among xylulose kinase, glycerol kinase, ribulose kinase and SePSK.	RESULTS
+124	139	ribulose kinase	protein_type	To understand the catalytic mechanism of SePSK, we performed structural comparisons among xylulose kinase, glycerol kinase, ribulose kinase and SePSK.	RESULTS
+144	149	SePSK	protein	To understand the catalytic mechanism of SePSK, we performed structural comparisons among xylulose kinase, glycerol kinase, ribulose kinase and SePSK.	RESULTS
+53	55	D8	residue_name_number	Our results suggested that three conserved residues (D8, T11 and D221 of SePSK) play an important role in SePSK function.	RESULTS
+57	60	T11	residue_name_number	Our results suggested that three conserved residues (D8, T11 and D221 of SePSK) play an important role in SePSK function.	RESULTS
+65	69	D221	residue_name_number	Our results suggested that three conserved residues (D8, T11 and D221 of SePSK) play an important role in SePSK function.	RESULTS
+73	78	SePSK	protein	Our results suggested that three conserved residues (D8, T11 and D221 of SePSK) play an important role in SePSK function.	RESULTS
+106	111	SePSK	protein	Our results suggested that three conserved residues (D8, T11 and D221 of SePSK) play an important role in SePSK function.	RESULTS
+0	9	Mutations	experimental_method	Mutations of the corresponding residue in xylulose kinase and glycerol kinase from Escherichia coli greatly reduced their activity.	RESULTS
+42	57	xylulose kinase	protein_type	Mutations of the corresponding residue in xylulose kinase and glycerol kinase from Escherichia coli greatly reduced their activity.	RESULTS
+62	77	glycerol kinase	protein_type	Mutations of the corresponding residue in xylulose kinase and glycerol kinase from Escherichia coli greatly reduced their activity.	RESULTS
+83	99	Escherichia coli	species	Mutations of the corresponding residue in xylulose kinase and glycerol kinase from Escherichia coli greatly reduced their activity.	RESULTS
+52	57	SePSK	protein	To identify the function of these three residues of SePSK, we constructed D8A, T11A and D221A mutants.	RESULTS
+74	77	D8A	mutant	To identify the function of these three residues of SePSK, we constructed D8A, T11A and D221A mutants.	RESULTS
+79	83	T11A	mutant	To identify the function of these three residues of SePSK, we constructed D8A, T11A and D221A mutants.	RESULTS
+88	93	D221A	mutant	To identify the function of these three residues of SePSK, we constructed D8A, T11A and D221A mutants.	RESULTS
+94	101	mutants	protein_state	To identify the function of these three residues of SePSK, we constructed D8A, T11A and D221A mutants.	RESULTS
+6	31	enzymatic activity assays	experimental_method	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+99	102	ATP	chemical	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+127	137	D-ribulose	chemical	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+151	160	wild type	protein_state	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+256	271	phosphorylation	ptm	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+272	282	D-ribulose	chemical	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+317	322	SePSK	protein	Using enzymatic activity assays, we found that all of these mutants exhibit much lower activity of ATP hydrolysis after adding D-ribulose than that of wild type, indicating the possibility that these three residues are involved in the catalytic process of phosphorylation D-ribulose and are vital for the function of SePSK (Fig 2D).	RESULTS
+0	5	SePSK	protein	SePSK and AtXK-1 possess a similar ATP binding site	RESULTS
+10	16	AtXK-1	protein	SePSK and AtXK-1 possess a similar ATP binding site	RESULTS
+35	51	ATP binding site	site	SePSK and AtXK-1 possess a similar ATP binding site	RESULTS
+39	44	SePSK	protein	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+49	55	AtXK-1	protein	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+56	71	in complex with	protein_state	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+72	75	ATP	chemical	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+80	86	soaked	experimental_method	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+91	94	apo	protein_state	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+95	103	crystals	evidence	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+137	140	ATP	chemical	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+159	169	structures	evidence	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+173	178	SePSK	protein	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+183	189	AtXK-1	protein	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+190	200	bound with	protein_state	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+201	204	ATP	chemical	To obtain more detailed information of SePSK and AtXK-1 in complex with ATP, we soaked the apo-crystals in the reservoir adding cofactor ATP, and obtained the structures of SePSK and AtXK-1 bound with ATP at the resolution of 2.3 Å and 1.8 Å, respectively.	RESULTS
+8	18	structures	evidence	In both structures, a strong electron density was found in the conserved ATP binding pocket, but can only be fitted with an ADP molecule (S4 Fig).	RESULTS
+29	45	electron density	evidence	In both structures, a strong electron density was found in the conserved ATP binding pocket, but can only be fitted with an ADP molecule (S4 Fig).	RESULTS
+63	72	conserved	protein_state	In both structures, a strong electron density was found in the conserved ATP binding pocket, but can only be fitted with an ADP molecule (S4 Fig).	RESULTS
+73	91	ATP binding pocket	site	In both structures, a strong electron density was found in the conserved ATP binding pocket, but can only be fitted with an ADP molecule (S4 Fig).	RESULTS
+124	127	ADP	chemical	In both structures, a strong electron density was found in the conserved ATP binding pocket, but can only be fitted with an ADP molecule (S4 Fig).	RESULTS
+13	23	structures	evidence	Thus the two structures were named ADP-SePSK and ADP-AtXK-1, respectively.	RESULTS
+35	44	ADP-SePSK	complex_assembly	Thus the two structures were named ADP-SePSK and ADP-AtXK-1, respectively.	RESULTS
+49	59	ADP-AtXK-1	complex_assembly	Thus the two structures were named ADP-SePSK and ADP-AtXK-1, respectively.	RESULTS
+19	37	electron densities	evidence	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+47	56	phosphate	chemical	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+65	75	structures	evidence	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+95	104	phosphate	chemical	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+114	117	ATP	chemical	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+154	159	SePSK	protein	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+164	170	AtXK-1	protein	The extremely weak electron densities of ATP γ-phosphate in both structures suggest that the γ-phosphate group of ATP is either flexible or hydrolyzed by SePSK and AtXK-1.	RESULTS
+36	61	enzymatic activity assays	experimental_method	This result was consistent with our enzymatic activity assays where SePSK and AtXK-1 showed ATP hydrolysis activity without adding any substrates (Fig 2A and 2C).	RESULTS
+68	73	SePSK	protein	This result was consistent with our enzymatic activity assays where SePSK and AtXK-1 showed ATP hydrolysis activity without adding any substrates (Fig 2A and 2C).	RESULTS
+78	84	AtXK-1	protein	This result was consistent with our enzymatic activity assays where SePSK and AtXK-1 showed ATP hydrolysis activity without adding any substrates (Fig 2A and 2C).	RESULTS
+92	95	ATP	chemical	This result was consistent with our enzymatic activity assays where SePSK and AtXK-1 showed ATP hydrolysis activity without adding any substrates (Fig 2A and 2C).	RESULTS
+23	26	ATP	chemical	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+31	37	soaked	experimental_method	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+42	50	crystals	evidence	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+54	57	apo	protein_state	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+58	63	SePSK	protein	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+68	71	apo	protein_state	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+72	78	AtXK-1	protein	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+105	112	AMP-PNP	chemical	To avoid hydrolysis of ATP, we soaked the crystals of apo-SePSK and apo-AtXK-1 into the reservoir adding AMP-PNP.	RESULTS
+27	45	electron densities	evidence	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+51	60	phosphate	chemical	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+70	77	AMP-PNP	chemical	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+79	86	AMP-PNP	chemical	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+89	98	phosphate	chemical	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+122	135	AMP-PNP-SePSK	complex_assembly	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+140	154	AMP-PNP-AtXK-1	complex_assembly	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+155	165	structures	evidence	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+198	201	ATP	chemical	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+204	213	phosphate	chemical	However, we found that the electron densities of γ-phosphate group of AMP-PNP (AMP-PNP γ-phosphate) are still weak in the AMP-PNP-SePSK and AMP-PNP-AtXK-1 structures, suggesting high flexibility of ATP-γ-phosphate.	RESULTS
+6	15	phosphate	chemical	The γ-phosphate group of ATP is transferred to the sugar substrate during the reaction process, so this flexibility might be important for the ability of these kinases.	RESULTS
+25	28	ATP	chemical	The γ-phosphate group of ATP is transferred to the sugar substrate during the reaction process, so this flexibility might be important for the ability of these kinases.	RESULTS
+51	56	sugar	chemical	The γ-phosphate group of ATP is transferred to the sugar substrate during the reaction process, so this flexibility might be important for the ability of these kinases.	RESULTS
+160	167	kinases	protein_type	The γ-phosphate group of ATP is transferred to the sugar substrate during the reaction process, so this flexibility might be important for the ability of these kinases.	RESULTS
+12	22	structures	evidence	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+60	63	ADP	chemical	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+68	75	AMP-PNP	chemical	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+83	97	AMP-PNP-AtXK-1	complex_assembly	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+99	109	ADP-AtXK-1	complex_assembly	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+111	120	ADP-SePSK	complex_assembly	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+125	138	AMP-PNP-SePSK	complex_assembly	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+139	149	structures	evidence	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+195	204	structure	evidence	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+208	221	AMP-PNP-SePSK	complex_assembly	The overall structures as well as the coordination modes of ADP and AMP-PNP in the AMP-PNP-AtXK-1, ADP-AtXK-1, ADP-SePSK and AMP-PNP-SePSK structures are nearly identical (S5 Fig), therefore the structure of AMP-PNP-SePSK is used here to describe the structural details and to compare with those of other family members.	RESULTS
+24	29	SePSK	protein	As shown in Fig 3A, one SePSK protein molecule is in an asymmetric unit with one AMP-PNP molecule.	RESULTS
+81	88	AMP-PNP	chemical	As shown in Fig 3A, one SePSK protein molecule is in an asymmetric unit with one AMP-PNP molecule.	RESULTS
+4	11	AMP-PNP	chemical	The AMP-PNP is bound at the domain II, where it fits well inside a positively charged groove.	RESULTS
+28	37	domain II	structure_element	The AMP-PNP is bound at the domain II, where it fits well inside a positively charged groove.	RESULTS
+67	92	positively charged groove	site	The AMP-PNP is bound at the domain II, where it fits well inside a positively charged groove.	RESULTS
+4	26	AMP-PNP binding pocket	site	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+39	53	four α-helices	structure_element	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+55	58	α26	structure_element	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+60	63	α28	structure_element	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+65	68	α27	structure_element	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+73	76	α30	structure_element	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+90	118	shape resembling a half-fist	protein_state	The AMP-PNP binding pocket consists of four α-helices (α26, α28, α27 and α30) and forms a shape resembling a half-fist (Fig 3A and 3B).	RESULTS
+22	29	AMP-PNP	chemical	The head group of the AMP-PNP is embedded in a pocket surrounded by Trp383, Asn380, Gly376 and Gly377.	RESULTS
+47	53	pocket	site	The head group of the AMP-PNP is embedded in a pocket surrounded by Trp383, Asn380, Gly376 and Gly377.	RESULTS
+68	74	Trp383	residue_name_number	The head group of the AMP-PNP is embedded in a pocket surrounded by Trp383, Asn380, Gly376 and Gly377.	RESULTS
+76	82	Asn380	residue_name_number	The head group of the AMP-PNP is embedded in a pocket surrounded by Trp383, Asn380, Gly376 and Gly377.	RESULTS
+84	90	Gly376	residue_name_number	The head group of the AMP-PNP is embedded in a pocket surrounded by Trp383, Asn380, Gly376 and Gly377.	RESULTS
+95	101	Gly377	residue_name_number	The head group of the AMP-PNP is embedded in a pocket surrounded by Trp383, Asn380, Gly376 and Gly377.	RESULTS
+19	26	AMP-PNP	chemical	The purine ring of AMP-PNP is positioned in parallel to the indole ring of Trp383.	RESULTS
+75	81	Trp383	residue_name_number	The purine ring of AMP-PNP is positioned in parallel to the indole ring of Trp383.	RESULTS
+64	70	Asn380	residue_name_number	In addition, it is hydrogen-bonded with the side chain amide of Asn380 (Fig 3B).	RESULTS
+12	19	AMP-PNP	chemical	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+34	46	hinge region	structure_element	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+50	55	SePSK	protein	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+67	76	phosphate	chemical	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+83	92	phosphate	chemical	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+118	124	Gly376	residue_name_number	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+129	135	Ser243	residue_name_number	The tail of AMP-PNP points to the hinge region of SePSK, and its α-phosphate and β-phosphate groups are stabilized by Gly376 and Ser243, respectively.	RESULTS
+15	24	structure	evidence	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+48	55	AMP-PNP	chemical	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+58	67	phosphate	chemical	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+91	109	ATP binding pocket	site	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+122	131	phosphate	chemical	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+168	176	domain I	structure_element	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+181	190	domain II	structure_element	Together, this structure clearly shows that the AMP-PNP-β-phosphate is sticking out of the ATP binding pocket, thus the γ-phosphate group is at the empty space between domain I and domain II and is unconstrained in its movement by the protein.	RESULTS
+0	9	Structure	evidence	Structure of SePSK in complex with AMP-PNP.	FIG
+13	18	SePSK	protein	Structure of SePSK in complex with AMP-PNP.	FIG
+19	34	in complex with	protein_state	Structure of SePSK in complex with AMP-PNP.	FIG
+35	42	AMP-PNP	chemical	Structure of SePSK in complex with AMP-PNP.	FIG
+8	24	electron density	evidence	(A) The electron density of AMP-PNP.	FIG
+28	35	AMP-PNP	chemical	(A) The electron density of AMP-PNP.	FIG
+4	9	SePSK	protein	The SePSK structure is shown in the electrostatic potential surface mode.	FIG
+10	19	structure	evidence	The SePSK structure is shown in the electrostatic potential surface mode.	FIG
+4	11	AMP-PNP	chemical	The AMP-PNP is depicted as sticks with its ǀFoǀ-ǀFcǀ map contoured at 3 σ shown as cyan mesh.	FIG
+43	56	ǀFoǀ-ǀFcǀ map	evidence	The AMP-PNP is depicted as sticks with its ǀFoǀ-ǀFcǀ map contoured at 3 σ shown as cyan mesh.	FIG
+8	30	AMP-PNP binding pocket	site	(B) The AMP-PNP binding pocket.	FIG
+12	19	AMP-PNP	chemical	The head of AMP-PNP is sandwiched by four residues (Leu293, Gly376, Gly377 and Trp383).	FIG
+52	58	Leu293	residue_name_number	The head of AMP-PNP is sandwiched by four residues (Leu293, Gly376, Gly377 and Trp383).	FIG
+60	66	Gly376	residue_name_number	The head of AMP-PNP is sandwiched by four residues (Leu293, Gly376, Gly377 and Trp383).	FIG
+68	74	Gly377	residue_name_number	The head of AMP-PNP is sandwiched by four residues (Leu293, Gly376, Gly377 and Trp383).	FIG
+79	85	Trp383	residue_name_number	The head of AMP-PNP is sandwiched by four residues (Leu293, Gly376, Gly377 and Trp383).	FIG
+9	18	α-helices	structure_element	The four α-helices (α26, α28, α27 and α30) are labeled in red.	FIG
+20	23	α26	structure_element	The four α-helices (α26, α28, α27 and α30) are labeled in red.	FIG
+25	28	α28	structure_element	The four α-helices (α26, α28, α27 and α30) are labeled in red.	FIG
+30	33	α27	structure_element	The four α-helices (α26, α28, α27 and α30) are labeled in red.	FIG
+38	41	α30	structure_element	The four α-helices (α26, α28, α27 and α30) are labeled in red.	FIG
+4	11	AMP-PNP	chemical	The AMP-PNP and coordinated residues are shown as sticks.	FIG
+14	36	substrate binding site	site	The potential substrate binding site in SePSK	RESULTS
+40	45	SePSK	protein	The potential substrate binding site in SePSK	RESULTS
+21	36	activity assays	experimental_method	The results from our activity assays suggested that SePSK has D-ribulose kinase activity.	RESULTS
+52	57	SePSK	protein	The results from our activity assays suggested that SePSK has D-ribulose kinase activity.	RESULTS
+62	79	D-ribulose kinase	protein_type	The results from our activity assays suggested that SePSK has D-ribulose kinase activity.	RESULTS
+53	58	SePSK	protein	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+63	73	D-ribulose	chemical	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+79	82	apo	protein_state	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+83	88	SePSK	protein	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+89	114	crystals were soaked into	experimental_method	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+119	128	reservoir	experimental_method	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+140	150	D-ribulose	chemical	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+152	155	RBL	chemical	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+165	174	RBL-SePSK	complex_assembly	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+175	184	structure	evidence	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+189	195	solved	experimental_method	To better understand the interaction pattern between SePSK and D-ribulose, the apo-SePSK crystals were soaked into the reservoir with 10 mM D-ribulose (RBL) and the RBL-SePSK structure was solved.	RESULTS
+33	51	electron densities	evidence	As shown in S6 Fig, two residual electron densities are visible in domain I, which can be interpreted as two D-ribulose molecules with reasonable fit.	RESULTS
+67	75	domain I	structure_element	As shown in S6 Fig, two residual electron densities are visible in domain I, which can be interpreted as two D-ribulose molecules with reasonable fit.	RESULTS
+109	119	D-ribulose	chemical	As shown in S6 Fig, two residual electron densities are visible in domain I, which can be interpreted as two D-ribulose molecules with reasonable fit.	RESULTS
+76	86	D-ribulose	chemical	As shown in Fig 4A, the nearest distance between the carbon skeleton of two D-ribulose molecules are approx.	RESULTS
+7	11	RBL1	residue_name_number	7.1 Å (RBL1-C4 and RBL2-C1).	RESULTS
+19	23	RBL2	residue_name_number	7.1 Å (RBL1-C4 and RBL2-C1).	RESULTS
+0	4	RBL1	residue_name_number	RBL1 is located in the pocket consisting of α21 and the loop between β6 and β7.	RESULTS
+23	29	pocket	site	RBL1 is located in the pocket consisting of α21 and the loop between β6 and β7.	RESULTS
+44	47	α21	structure_element	RBL1 is located in the pocket consisting of α21 and the loop between β6 and β7.	RESULTS
+56	60	loop	structure_element	RBL1 is located in the pocket consisting of α21 and the loop between β6 and β7.	RESULTS
+69	78	β6 and β7	structure_element	RBL1 is located in the pocket consisting of α21 and the loop between β6 and β7.	RESULTS
+17	21	RBL1	residue_name_number	The O4 and O5 of RBL1 are coordinated with the side chain carboxyl group of Asp221.	RESULTS
+76	82	Asp221	residue_name_number	The O4 and O5 of RBL1 are coordinated with the side chain carboxyl group of Asp221.	RESULTS
+23	27	RBL1	residue_name_number	Furthermore, the O2 of RBL1 interacts with the main chain amide nitrogen of Ser72 (Fig 4B).	RESULTS
+76	81	Ser72	residue_name_number	Furthermore, the O2 of RBL1 interacts with the main chain amide nitrogen of Ser72 (Fig 4B).	RESULTS
+5	11	pocket	site	This pocket is at a similar position of substrate binding site of other sugar kinase, such as L-ribulokinase (PDB code: 3QDK) (S7 Fig).	RESULTS
+40	62	substrate binding site	site	This pocket is at a similar position of substrate binding site of other sugar kinase, such as L-ribulokinase (PDB code: 3QDK) (S7 Fig).	RESULTS
+72	84	sugar kinase	protein_type	This pocket is at a similar position of substrate binding site of other sugar kinase, such as L-ribulokinase (PDB code: 3QDK) (S7 Fig).	RESULTS
+94	108	L-ribulokinase	protein	This pocket is at a similar position of substrate binding site of other sugar kinase, such as L-ribulokinase (PDB code: 3QDK) (S7 Fig).	RESULTS
+9	30	structural comparison	experimental_method	However, structural comparison shows that the substrate ligating residues between the two structures are not strictly conserved.	RESULTS
+90	100	structures	evidence	However, structural comparison shows that the substrate ligating residues between the two structures are not strictly conserved.	RESULTS
+105	127	not strictly conserved	protein_state	However, structural comparison shows that the substrate ligating residues between the two structures are not strictly conserved.	RESULTS
+13	23	structures	evidence	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+50	54	RBL1	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+58	67	RBL-SePSK	complex_assembly	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+68	77	structure	evidence	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+82	87	Ser72	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+89	95	Asp221	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+100	106	Ser222	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+140	150	L-ribulose	chemical	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+156	170	L-ribulokinase	protein	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+175	180	Ala96	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+182	188	Lys208	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+190	196	Asp274	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+201	207	Glu329	residue_name_number	Based on the structures, the ligating residues of RBL1 in RBL-SePSK structure are Ser72, Asp221 and Ser222, and the interacting residues of L-ribulose with L-ribulokinase are Ala96, Lys208, Asp274 and Glu329 (S7 Fig).	RESULTS
+0	6	Glu329	residue_name_number	Glu329 in 3QDK has no counterpart in RBL-SePSK structure.	RESULTS
+37	46	RBL-SePSK	complex_assembly	Glu329 in 3QDK has no counterpart in RBL-SePSK structure.	RESULTS
+47	56	structure	evidence	Glu329 in 3QDK has no counterpart in RBL-SePSK structure.	RESULTS
+22	28	Lys208	residue_name_number	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+32	46	L-ribulokinase	protein	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+78	84	Lys163	residue_name_number	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+89	98	RBL-SePSK	complex_assembly	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+99	108	structure	evidence	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+131	137	Lys163	residue_name_number	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+192	201	α-helices	structure_element	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+203	205	α9	structure_element	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+210	213	α13	structure_element	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+218	223	SePSK	protein	In addition, although Lys208 of L-ribulokinase has the corresponding residue (Lys163) in RBL-SePSK structure, the hydrogen bond of Lys163 is broken because of the conformational change of two α-helices (α9 and α13) of SePSK.	RESULTS
+15	25	D-ribulose	chemical	The binding of D-ribulose (RBL) with SePSK.	FIG
+27	30	RBL	chemical	The binding of D-ribulose (RBL) with SePSK.	FIG
+37	42	SePSK	protein	The binding of D-ribulose (RBL) with SePSK.	FIG
+8	43	electrostatic potential surface map	evidence	(A) The electrostatic potential surface map of RBL-SePSK and a zoom-in view of RBL binding site.	FIG
+47	56	RBL-SePSK	complex_assembly	(A) The electrostatic potential surface map of RBL-SePSK and a zoom-in view of RBL binding site.	FIG
+79	95	RBL binding site	site	(A) The electrostatic potential surface map of RBL-SePSK and a zoom-in view of RBL binding site.	FIG
+4	8	RBL1	residue_name_number	The RBL1 and RBL2 are depicted as sticks. (B) Interaction of two D-ribulose molecules (RBL1 and RBL2) with SePSK.	FIG
+13	17	RBL2	residue_name_number	The RBL1 and RBL2 are depicted as sticks. (B) Interaction of two D-ribulose molecules (RBL1 and RBL2) with SePSK.	FIG
+65	75	D-ribulose	chemical	The RBL1 and RBL2 are depicted as sticks. (B) Interaction of two D-ribulose molecules (RBL1 and RBL2) with SePSK.	FIG
+87	91	RBL1	residue_name_number	The RBL1 and RBL2 are depicted as sticks. (B) Interaction of two D-ribulose molecules (RBL1 and RBL2) with SePSK.	FIG
+96	100	RBL2	residue_name_number	The RBL1 and RBL2 are depicted as sticks. (B) Interaction of two D-ribulose molecules (RBL1 and RBL2) with SePSK.	FIG
+107	112	SePSK	protein	The RBL1 and RBL2 are depicted as sticks. (B) Interaction of two D-ribulose molecules (RBL1 and RBL2) with SePSK.	FIG
+4	7	RBL	chemical	The RBL molecules (carbon atoms colored yellow) and amino acid residues of SePSK (carbon atoms colored green) involved in RBL interaction are shown as sticks.	FIG
+75	80	SePSK	protein	The RBL molecules (carbon atoms colored yellow) and amino acid residues of SePSK (carbon atoms colored green) involved in RBL interaction are shown as sticks.	FIG
+122	125	RBL	chemical	The RBL molecules (carbon atoms colored yellow) and amino acid residues of SePSK (carbon atoms colored green) involved in RBL interaction are shown as sticks.	FIG
+128	151	binding affinity assays	experimental_method	The hydrogen bonds are indicated by the black dashed lines and the numbers near the dashed lines are the distances (Å). (C) The binding affinity assays of SePSK with D-ribulose.	FIG
+155	160	SePSK	protein	The hydrogen bonds are indicated by the black dashed lines and the numbers near the dashed lines are the distances (Å). (C) The binding affinity assays of SePSK with D-ribulose.	FIG
+166	176	D-ribulose	chemical	The hydrogen bonds are indicated by the black dashed lines and the numbers near the dashed lines are the distances (Å). (C) The binding affinity assays of SePSK with D-ribulose.	FIG
+0	25	Single-cycle kinetic data	experimental_method	Single-cycle kinetic data are reflecting the interaction of SePSK and D8A-SePSK with D-ribulose.	FIG
+60	65	SePSK	protein	Single-cycle kinetic data are reflecting the interaction of SePSK and D8A-SePSK with D-ribulose.	FIG
+70	73	D8A	mutant	Single-cycle kinetic data are reflecting the interaction of SePSK and D8A-SePSK with D-ribulose.	FIG
+74	79	SePSK	protein	Single-cycle kinetic data are reflecting the interaction of SePSK and D8A-SePSK with D-ribulose.	FIG
+85	95	D-ribulose	chemical	Single-cycle kinetic data are reflecting the interaction of SePSK and D8A-SePSK with D-ribulose.	FIG
+26	37	sensorgrams	evidence	It shows two experimental sensorgrams after minus the empty sensorgrams.	FIG
+60	71	sensorgrams	evidence	It shows two experimental sensorgrams after minus the empty sensorgrams.	FIG
+92	101	wild type	protein_state	The original data is shown as black curve, and the fitted data is shown as different color (wild type SePSK: red curve, D8A-SePSK: green curve).	FIG
+102	107	SePSK	protein	The original data is shown as black curve, and the fitted data is shown as different color (wild type SePSK: red curve, D8A-SePSK: green curve).	FIG
+120	123	D8A	mutant	The original data is shown as black curve, and the fitted data is shown as different color (wild type SePSK: red curve, D8A-SePSK: green curve).	FIG
+124	129	SePSK	protein	The original data is shown as black curve, and the fitted data is shown as different color (wild type SePSK: red curve, D8A-SePSK: green curve).	FIG
+0	26	Dissociation rate constant	evidence	Dissociation rate constant of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	FIG
+30	39	wild type	protein_state	Dissociation rate constant of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	FIG
+44	47	D8A	mutant	Dissociation rate constant of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	FIG
+48	53	SePSK	protein	Dissociation rate constant of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	FIG
+4	18	binding pocket	site	The binding pocket of RBL2 with relatively weak electron density is near the N-terminal region of SePSK and is negatively charged.	RESULTS
+22	26	RBL2	residue_name_number	The binding pocket of RBL2 with relatively weak electron density is near the N-terminal region of SePSK and is negatively charged.	RESULTS
+48	64	electron density	evidence	The binding pocket of RBL2 with relatively weak electron density is near the N-terminal region of SePSK and is negatively charged.	RESULTS
+98	103	SePSK	protein	The binding pocket of RBL2 with relatively weak electron density is near the N-terminal region of SePSK and is negatively charged.	RESULTS
+18	22	Asp8	residue_name_number	The side chain of Asp8 interacts strongly with O3 and O4 of RBL2.	RESULTS
+60	64	RBL2	residue_name_number	The side chain of Asp8 interacts strongly with O3 and O4 of RBL2.	RESULTS
+22	27	Ser12	residue_name_number	The hydroxyl group of Ser12 coordinates with O2 of RBL2.	RESULTS
+51	55	RBL2	residue_name_number	The hydroxyl group of Ser12 coordinates with O2 of RBL2.	RESULTS
+32	37	Gly13	residue_name_number	The backbone amide nitrogens of Gly13 and Arg15 also keep hydrogen bonds with RBL2 (Fig 4B).	RESULTS
+42	47	Arg15	residue_name_number	The backbone amide nitrogens of Gly13 and Arg15 also keep hydrogen bonds with RBL2 (Fig 4B).	RESULTS
+78	82	RBL2	residue_name_number	The backbone amide nitrogens of Gly13 and Arg15 also keep hydrogen bonds with RBL2 (Fig 4B).	RESULTS
+0	21	Structural comparison	experimental_method	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+25	30	SePSK	protein	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+35	41	AtXK-1	protein	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+64	83	RBL1 binding pocket	site	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+87	96	conserved	protein_state	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+102	113	RBL2 pocket	site	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+130	136	AtXK-1	protein	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+137	146	structure	evidence	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+200	204	RBL2	residue_name_number	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+209	225	highly conserved	protein_state	Structural comparison of SePSK and AtXK-1 showed that while the RBL1 binding pocket is conserved, the RBL2 pocket is disrupted in AtXK-1 structure, despite the fact that the residues interacting with RBL2 are highly conserved between the two proteins.	RESULTS
+7	16	RBL-SePSK	complex_assembly	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+17	26	structure	evidence	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+69	73	RBL2	residue_name_number	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+78	83	Ser12	residue_name_number	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+107	113	AtXK-1	protein	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+114	123	structure	evidence	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+175	180	Ser22	residue_name_number	In the RBL-SePSK structure, a 2.6 Å hydrogen bond is present between RBL2 and Ser12 (Fig 4B), while in the AtXK-1 structure this hydrogen bond with the corresponding residue (Ser22) is broken.	RESULTS
+71	79	β-sheets	structure_element	This break is probably induced by the conformational change of the two β-sheets (β1 and β2), with the result that the linking loop (loop 1) is located further away from the RBL2 binding site.	RESULTS
+81	83	β1	structure_element	This break is probably induced by the conformational change of the two β-sheets (β1 and β2), with the result that the linking loop (loop 1) is located further away from the RBL2 binding site.	RESULTS
+88	90	β2	structure_element	This break is probably induced by the conformational change of the two β-sheets (β1 and β2), with the result that the linking loop (loop 1) is located further away from the RBL2 binding site.	RESULTS
+118	130	linking loop	structure_element	This break is probably induced by the conformational change of the two β-sheets (β1 and β2), with the result that the linking loop (loop 1) is located further away from the RBL2 binding site.	RESULTS
+132	138	loop 1	structure_element	This break is probably induced by the conformational change of the two β-sheets (β1 and β2), with the result that the linking loop (loop 1) is located further away from the RBL2 binding site.	RESULTS
+173	190	RBL2 binding site	site	This break is probably induced by the conformational change of the two β-sheets (β1 and β2), with the result that the linking loop (loop 1) is located further away from the RBL2 binding site.	RESULTS
+37	43	AtXK-1	protein	This change might be the reason that AtXK-1 only shows limited increasing in its ATP hydrolysis ability upon adding D-ribulose as a substrate after comparing with SePSK (Fig 2C).	RESULTS
+81	84	ATP	chemical	This change might be the reason that AtXK-1 only shows limited increasing in its ATP hydrolysis ability upon adding D-ribulose as a substrate after comparing with SePSK (Fig 2C).	RESULTS
+116	126	D-ribulose	chemical	This change might be the reason that AtXK-1 only shows limited increasing in its ATP hydrolysis ability upon adding D-ribulose as a substrate after comparing with SePSK (Fig 2C).	RESULTS
+163	168	SePSK	protein	This change might be the reason that AtXK-1 only shows limited increasing in its ATP hydrolysis ability upon adding D-ribulose as a substrate after comparing with SePSK (Fig 2C).	RESULTS
+4	9	SePSK	protein	Our SePSK structure shows that the Asp8 residue forms strong hydrogen bond with RBL2 (Fig 4B).	RESULTS
+10	19	structure	evidence	Our SePSK structure shows that the Asp8 residue forms strong hydrogen bond with RBL2 (Fig 4B).	RESULTS
+35	39	Asp8	residue_name_number	Our SePSK structure shows that the Asp8 residue forms strong hydrogen bond with RBL2 (Fig 4B).	RESULTS
+80	84	RBL2	residue_name_number	Our SePSK structure shows that the Asp8 residue forms strong hydrogen bond with RBL2 (Fig 4B).	RESULTS
+17	33	enzymatic assays	experimental_method	In addition, our enzymatic assays indicated that Asp8 is important for the activity of SePSK (Fig 2D).	RESULTS
+49	53	Asp8	residue_name_number	In addition, our enzymatic assays indicated that Asp8 is important for the activity of SePSK (Fig 2D).	RESULTS
+87	92	SePSK	protein	In addition, our enzymatic assays indicated that Asp8 is important for the activity of SePSK (Fig 2D).	RESULTS
+49	65	binding affinity	evidence	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+70	80	D-ribulose	chemical	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+89	98	wild type	protein_state	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+100	102	WT	protein_state	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+108	111	D8A	mutant	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+112	118	mutant	protein_state	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+122	127	SePSK	protein	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+136	168	surface plasmon resonance method	experimental_method	To further verified this result, we measured the binding affinity for D-ribulose of both wild type (WT) and D8A mutant of SePSK using a surface plasmon resonance method.	RESULTS
+28	36	affinity	evidence	The results showed that the affinity of D8A-SePSK with D-ribulose is weaker than that of WT with a reduction of approx.	RESULTS
+40	43	D8A	mutant	The results showed that the affinity of D8A-SePSK with D-ribulose is weaker than that of WT with a reduction of approx.	RESULTS
+44	49	SePSK	protein	The results showed that the affinity of D8A-SePSK with D-ribulose is weaker than that of WT with a reduction of approx.	RESULTS
+55	65	D-ribulose	chemical	The results showed that the affinity of D8A-SePSK with D-ribulose is weaker than that of WT with a reduction of approx.	RESULTS
+89	91	WT	protein_state	The results showed that the affinity of D8A-SePSK with D-ribulose is weaker than that of WT with a reduction of approx.	RESULTS
+0	26	Dissociation rate constant	evidence	Dissociation rate constant (Kd) of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	RESULTS
+28	30	Kd	evidence	Dissociation rate constant (Kd) of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	RESULTS
+35	44	wild type	protein_state	Dissociation rate constant (Kd) of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	RESULTS
+49	52	D8A	mutant	Dissociation rate constant (Kd) of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	RESULTS
+53	58	SePSK	protein	Dissociation rate constant (Kd) of wild type and D8A-SePSK are 3 ms-1 and 9 ms-1, respectively.	RESULTS
+29	52	second RBL binding site	site	The results implied that the second RBL binding site plays a role in the D-ribulose kinase function of SePSK.	RESULTS
+73	90	D-ribulose kinase	protein_type	The results implied that the second RBL binding site plays a role in the D-ribulose kinase function of SePSK.	RESULTS
+103	108	SePSK	protein	The results implied that the second RBL binding site plays a role in the D-ribulose kinase function of SePSK.	RESULTS
+47	57	D-ribulose	chemical	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+67	82	crystal soaking	experimental_method	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+115	131	electron density	evidence	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+135	139	RBL2	residue_name_number	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+170	189	second binding site	site	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+193	203	D-ribulose	chemical	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+207	212	SePSK	protein	However, considering the high concentration of D-ribulose used for crystal soaking, as well as the relatively weak electron density of RBL2, it is also possible that the second binding site of D-ribulose in SePSK is an artifact.	RESULTS
+35	40	SePSK	protein	Simulated conformational change of SePSK during the catalytic process	RESULTS
+60	68	domain I	structure_element	It was reported earlier that the crossing angle between the domain I and domain II in FGGY family carbohydrate kinases is different.	RESULTS
+73	82	domain II	structure_element	It was reported earlier that the crossing angle between the domain I and domain II in FGGY family carbohydrate kinases is different.	RESULTS
+86	118	FGGY family carbohydrate kinases	protein_type	It was reported earlier that the crossing angle between the domain I and domain II in FGGY family carbohydrate kinases is different.	RESULTS
+79	82	ATP	chemical	In addition, this difference may be caused by the binding of substrates and/or ATP.	RESULTS
+39	51	sugar kinase	protein_type	As reported previously, members of the sugar kinase family undergo a conformational change to narrow the crossing angle between two domains and reduce the distance between substrate and ATP in order to facilitate the catalytic reaction of phosphorylation of sugar substrates.	RESULTS
+186	189	ATP	chemical	As reported previously, members of the sugar kinase family undergo a conformational change to narrow the crossing angle between two domains and reduce the distance between substrate and ATP in order to facilitate the catalytic reaction of phosphorylation of sugar substrates.	RESULTS
+239	254	phosphorylation	ptm	As reported previously, members of the sugar kinase family undergo a conformational change to narrow the crossing angle between two domains and reduce the distance between substrate and ATP in order to facilitate the catalytic reaction of phosphorylation of sugar substrates.	RESULTS
+16	26	structures	evidence	After comparing structures of apo-SePSK, RBL-SePSK and AMP-PNP-SePSK, we noticed that these structures presented here are similar.	RESULTS
+30	33	apo	protein_state	After comparing structures of apo-SePSK, RBL-SePSK and AMP-PNP-SePSK, we noticed that these structures presented here are similar.	RESULTS
+34	39	SePSK	protein	After comparing structures of apo-SePSK, RBL-SePSK and AMP-PNP-SePSK, we noticed that these structures presented here are similar.	RESULTS
+41	50	RBL-SePSK	complex_assembly	After comparing structures of apo-SePSK, RBL-SePSK and AMP-PNP-SePSK, we noticed that these structures presented here are similar.	RESULTS
+55	68	AMP-PNP-SePSK	complex_assembly	After comparing structures of apo-SePSK, RBL-SePSK and AMP-PNP-SePSK, we noticed that these structures presented here are similar.	RESULTS
+92	102	structures	evidence	After comparing structures of apo-SePSK, RBL-SePSK and AMP-PNP-SePSK, we noticed that these structures presented here are similar.	RESULTS
+0	11	Superposing	experimental_method	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+16	26	structures	evidence	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+30	39	RBL-SePSK	complex_assembly	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+44	57	AMP-PNP-SePSK	complex_assembly	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+110	117	AMP-PNP	chemical	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+120	129	phosphate	chemical	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+134	138	RBL1	residue_name_number	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+139	143	RBL2	residue_name_number	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+154	158	RBL1	residue_name_number	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+170	174	RBL2	residue_name_number	Superposing the structures of RBL-SePSK and AMP-PNP-SePSK, the results show that the nearest distance between AMP-PNP γ-phosphate and RBL1/RBL2 is 7.5 Å (RBL1-O5)/6.7 Å (RBL2-O1) (S8 Fig).	RESULTS
+44	53	phosphate	chemical	This distance is too long to transfer the γ-phosphate group from ATP to the substrate.	RESULTS
+65	68	ATP	chemical	This distance is too long to transfer the γ-phosphate group from ATP to the substrate.	RESULTS
+25	30	SePSK	protein	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+60	69	structure	evidence	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+95	105	structures	evidence	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+109	114	SePSK	protein	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+129	133	open	protein_state	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+208	214	closed	protein_state	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+269	284	phosphorylation	ptm	Since the two domains of SePSK are widely separated in this structure, we hypothesize that our structures of SePSK represent its open form, and that a conformational rearrangement must occur to switch to the closed state in order to facilitate the catalytic process of phosphorylation of sugar substrates.	RESULTS
+53	63	simulation	experimental_method	For studying such potential conformational change, a simulation on the Hingeprot Server was performed to predict the movement of different SePSK domains.	RESULTS
+71	87	Hingeprot Server	experimental_method	For studying such potential conformational change, a simulation on the Hingeprot Server was performed to predict the movement of different SePSK domains.	RESULTS
+139	144	SePSK	protein	For studying such potential conformational change, a simulation on the Hingeprot Server was performed to predict the movement of different SePSK domains.	RESULTS
+24	32	domain I	structure_element	The results showed that domain I and domain II are closer to each other with Ala228 and Thr401 in A2 as Hinge-residues.	RESULTS
+37	46	domain II	structure_element	The results showed that domain I and domain II are closer to each other with Ala228 and Thr401 in A2 as Hinge-residues.	RESULTS
+77	83	Ala228	residue_name_number	The results showed that domain I and domain II are closer to each other with Ala228 and Thr401 in A2 as Hinge-residues.	RESULTS
+88	94	Thr401	residue_name_number	The results showed that domain I and domain II are closer to each other with Ala228 and Thr401 in A2 as Hinge-residues.	RESULTS
+98	100	A2	structure_element	The results showed that domain I and domain II are closer to each other with Ala228 and Thr401 in A2 as Hinge-residues.	RESULTS
+104	118	Hinge-residues	structure_element	The results showed that domain I and domain II are closer to each other with Ala228 and Thr401 in A2 as Hinge-residues.	RESULTS
+28	33	SePSK	protein	Based on the above results, SePSK is divided into two rigid parts.	RESULTS
+4	12	domain I	structure_element	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+16	25	RBL-SePSK	complex_assembly	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+31	36	1–228	residue_range	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+42	49	402–421	residue_range	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+59	68	domain II	structure_element	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+72	85	AMP-PNP-SePSK	complex_assembly	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+91	98	229–401	residue_range	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+105	115	superposed	experimental_method	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+121	131	structures	evidence	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+143	146	apo	protein_state	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+147	153	AtXK-1	protein	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+155	158	apo	protein_state	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+159	164	SePSK	protein	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+166	181	xylulose kinase	protein_type	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+187	212	Lactobacillus acidophilus	species	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+238	242	S58W	mutant	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+243	249	mutant	protein_state	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+258	273	glycerol kinase	protein_type	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+279	295	Escherichia coli	species	The domain I of RBL-SePSK (aa. 1–228, aa. 402–421) and the domain II of AMP-PNP-SePSK (aa. 229–401) were superposed with structures, including apo-AtXK-1, apo-SePSK, xylulose kinase from Lactobacillus acidophilus (PDB code: 3LL3) and the S58W mutant form of glycerol kinase from Escherichia coli (PDB code: 1GLJ).	RESULTS
+15	28	superposition	experimental_method	The results of superposition displayed different crossing angle between these two domains.	RESULTS
+6	19	superposition	experimental_method	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+38	45	AMP-PNP	chemical	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+48	57	phosphate	chemical	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+90	94	RBL1	residue_name_number	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+106	116	superposed	experimental_method	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+122	128	AtXK-1	protein	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+138	148	superposed	experimental_method	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+154	159	SePSK	protein	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+169	179	superposed	experimental_method	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+202	212	superposed	experimental_method	After superposition, the distances of AMP-PNP γ-phosphate and the fifth hydroxyl group of RBL1 are 7.9 Å (superposed with AtXK-1), 7.4 Å (superposed with SePSK), 6.6 Å (superposed with 3LL3) and 6.1 Å (superposed with 1GLJ).	RESULTS
+28	35	AMP-PNP	chemical	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+38	47	phosphate	chemical	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+80	84	RBL2	residue_name_number	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+96	106	superposed	experimental_method	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+112	118	AtXK-1	protein	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+128	138	superposed	experimental_method	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+144	149	SePSK	protein	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+159	169	superposed	experimental_method	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+188	195	AMP-PNP	chemical	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+198	207	phosphate	chemical	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+223	227	RBL2	residue_name_number	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+234	247	superposition	experimental_method	Meanwhile, the distances of AMP-PNP γ-phosphate and the first hydroxyl group of RBL2 are 7.2 Å (superposed with AtXK-1), 6.7 Å (superposed with SePSK), 3.7 Å (superposed with 3LL3), until AMP-PNP γ-phosphate fully contacts RBL2 after superposition with 1GLJ (Fig 5).	RESULTS
+22	26	RBL2	residue_name_number	This distance between RBL2 and AMP-PNP-γ-phosphate is close enough to facilitate phosphate transferring.	RESULTS
+31	38	AMP-PNP	chemical	This distance between RBL2 and AMP-PNP-γ-phosphate is close enough to facilitate phosphate transferring.	RESULTS
+41	50	phosphate	chemical	This distance between RBL2 and AMP-PNP-γ-phosphate is close enough to facilitate phosphate transferring.	RESULTS
+81	90	phosphate	chemical	This distance between RBL2 and AMP-PNP-γ-phosphate is close enough to facilitate phosphate transferring.	RESULTS
+14	27	superposition	experimental_method	Together, our superposition results provided snapshots of the conformational changes at different catalytic stages of SePSK and potentially revealed the closed form of SePSK.	RESULTS
+118	123	SePSK	protein	Together, our superposition results provided snapshots of the conformational changes at different catalytic stages of SePSK and potentially revealed the closed form of SePSK.	RESULTS
+153	159	closed	protein_state	Together, our superposition results provided snapshots of the conformational changes at different catalytic stages of SePSK and potentially revealed the closed form of SePSK.	RESULTS
+168	173	SePSK	protein	Together, our superposition results provided snapshots of the conformational changes at different catalytic stages of SePSK and potentially revealed the closed form of SePSK.	RESULTS
+35	40	SePSK	protein	Simulated conformational change of SePSK during the catalytic process.	FIG
+4	14	structures	evidence	The structures are shown as cartoon and the ligands are shown as sticks.	FIG
+0	8	Domain I	structure_element	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+14	30	D-ribulose-SePSK	complex_assembly	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+43	52	Domain II	structure_element	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+58	71	AMP-PNP-SePSK	complex_assembly	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+83	93	superposed	experimental_method	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+99	102	apo	protein_state	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+103	109	AtXK-1	protein	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+117	120	apo	protein_state	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+121	126	SePSK	protein	Domain I from D-ribulose-SePSK (green) and Domain II from AMP-PNP-SePSK (cyan) are superposed with apo-AtXK-1 (1st), apo-SePSK (2nd), 3LL3 (3rd) and 1GLJ (4th), respectively.	FIG
+92	95	RBL	chemical	The numbers near the black dashed lines show the distances (Å) between two nearest atoms of RBL and AMP-PNP.	FIG
+100	107	AMP-PNP	chemical	The numbers near the black dashed lines show the distances (Å) between two nearest atoms of RBL and AMP-PNP.	FIG
+16	49	structural and enzymatic analyses	experimental_method	In summary, our structural and enzymatic analyses provide evidence that SePSK shows D-ribulose kinase activity, and exhibits the conserved features of FGGY family carbohydrate kinases.	RESULTS
+72	77	SePSK	protein	In summary, our structural and enzymatic analyses provide evidence that SePSK shows D-ribulose kinase activity, and exhibits the conserved features of FGGY family carbohydrate kinases.	RESULTS
+84	101	D-ribulose kinase	protein_type	In summary, our structural and enzymatic analyses provide evidence that SePSK shows D-ribulose kinase activity, and exhibits the conserved features of FGGY family carbohydrate kinases.	RESULTS
+151	183	FGGY family carbohydrate kinases	protein_type	In summary, our structural and enzymatic analyses provide evidence that SePSK shows D-ribulose kinase activity, and exhibits the conserved features of FGGY family carbohydrate kinases.	RESULTS
+6	15	conserved	site	Three conserved residues in SePSK were identified to be essential for this function.	RESULTS
+28	33	SePSK	protein	Three conserved residues in SePSK were identified to be essential for this function.	RESULTS
+70	75	SePSK	protein	Our results provide the detailed information about the interaction of SePSK with ATP and substrates.	RESULTS
+81	84	ATP	chemical	Our results provide the detailed information about the interaction of SePSK with ATP and substrates.	RESULTS
+10	34	structural superposition	experimental_method	Moreover, structural superposition results enable us to visualize the conformational change of SePSK during the catalytic process.	RESULTS
+95	100	SePSK	protein	Moreover, structural superposition results enable us to visualize the conformational change of SePSK during the catalytic process.	RESULTS
+112	117	SePSK	protein	In conclusion, our results provide important information for a more detailed understanding of the mechanisms of SePSK and other members of FGGY family carbohydrate kinases.	RESULTS
+139	171	FGGY family carbohydrate kinases	protein_type	In conclusion, our results provide important information for a more detailed understanding of the mechanisms of SePSK and other members of FGGY family carbohydrate kinases.	RESULTS