|Journal of Structural Biology (2002) 139(3):161-70|
|Midwest Center for Structural Genomics|
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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.
|metabolism chemistry enzymology |
|Binding Sites Crystallography, X-Ray Humans Amino Acid Sequence Animals Models, Molecular Molecular Sequence Data Cloning, Molecular Protein Conformation Sequence Homology, Amino Acid Bacterial Proteins Structure-Activity Relationship Adenosine Triphosphate Phosphotransferases (Alcohol Group Acceptor) Evolution, Molecular Molecular Weight Bacillus subtilis Metals |
|13 (Last update: 08/11/2018 2:35:05pm)|
|J Struct Biol. 2002 Sep;139(3):161-70.|