annotation_CSV/PMC4880283.csv

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