1kyh: Difference between revisions

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==Overview==

We determined the 1.6-A resolution crystal structure of a conserved, hypothetical 29.9-kDa protein from the SIGY-CYDD intergenic region encoded, by a Bacillus subtilis open reading frame in the YXKO locus. YXKO, homologues are broadly distributed and are by and large described as, proteins with unknown function. The YXKO protein has an alpha/beta fold, and shows high structural homology to the members of a ribokinase-like, superfamily. However, YXKO is the only member of this superfamily known to, form tetramers. Putative binding sites for adenosine triphosphate (ATP), a, substrate, and Mg(2+)-binding sites were revealed in the structure of the, protein, based on high structural similarity to ATP-dependent members of, the superfamily. Two adjacent monomers contribute residues to the active, site. The crystal structure provides valuable information about the YXKO, protein's tertiary and quaternary structure, the biochemical function of, YXKO and its homologues, and the evolution of its ribokinase-like, superfamily.

We determined the 1.6-A resolution crystal structure of a conserved hypothetical 29.9-kDa protein from the SIGY-CYDD intergenic region encoded by a Bacillus subtilis open reading frame in the YXKO locus. YXKO homologues are broadly distributed and are by and large described as proteins with unknown function. The YXKO protein has an alpha/beta fold and shows high structural homology to the members of a ribokinase-like superfamily. However, YXKO is the only member of this superfamily known to form tetramers. Putative binding sites for adenosine triphosphate (ATP), a substrate, and Mg(2+)-binding sites were revealed in the structure of the protein, based on high structural similarity to ATP-dependent members of the superfamily. Two adjacent monomers contribute residues to the active site. The crystal structure provides valuable information about the YXKO protein's tertiary and quaternary structure, the biochemical function of YXKO and its homologues, and the evolution of its ribokinase-like superfamily.

==About this Structure==

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[[Category: Dementieva, I.]]

[[Category: Joachimiak, A.]]

[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]

[[Category: MCSG, Midwest Center for Structural Genomics.]]

[[Category: Vinokour, E.]]

[[Category: Zhang, R.]]

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[[Category: unknown function]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:17 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-We determined the 1.6-A resolution crystal structure of a conserved, hypothetical 29.9-kDa protein from the SIGY-CYDD intergenic region encoded, by a Bacillus subtilis open reading frame in the YXKO locus. YXKO, homologues are broadly distributed and are by and large described as, proteins with unknown function. The YXKO protein has an alpha/beta fold, and shows high structural homology to the members of a ribokinase-like, superfamily. However, YXKO is the only member of this superfamily known to, form tetramers. Putative binding sites for adenosine triphosphate (ATP), a, substrate, and Mg(2+)-binding sites were revealed in the structure of the, protein, based on high structural similarity to ATP-dependent members of, the superfamily. Two adjacent monomers contribute residues to the active, site. The crystal structure provides valuable information about the YXKO, protein's tertiary and quaternary structure, the biochemical function of, YXKO and its homologues, and the evolution of its ribokinase-like, superfamily.
+We determined the 1.6-A resolution crystal structure of a conserved hypothetical 29.9-kDa protein from the SIGY-CYDD intergenic region encoded by a Bacillus subtilis open reading frame in the YXKO locus. YXKO homologues are broadly distributed and are by and large described as proteins with unknown function. The YXKO protein has an alpha/beta fold and shows high structural homology to the members of a ribokinase-like superfamily. However, YXKO is the only member of this superfamily known to form tetramers. Putative binding sites for adenosine triphosphate (ATP), a substrate, and Mg(2+)-binding sites were revealed in the structure of the protein, based on high structural similarity to ATP-dependent members of the superfamily. Two adjacent monomers contribute residues to the active site. The crystal structure provides valuable information about the YXKO protein's tertiary and quaternary structure, the biochemical function of YXKO and its homologues, and the evolution of its ribokinase-like superfamily.
 ==About this Structure==
@@ Line 16: / Line 16: @@
 [[Category: Dementieva, I.]]
 [[Category: Joachimiak, A.]]
-[[Category: MCSG, Midwest.Center.for.Structural.Genomics.]]
+[[Category: MCSG, Midwest Center for Structural Genomics.]]
 [[Category: Vinokour, E.]]
 [[Category: Zhang, R.]]
@@ Line 26: / Line 26: @@
 [[Category: unknown function]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 11:49:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:39:17 2008''