1KYH
Structure of Bacillus subtilis YxkO, a Member of the UPF0031 Family and a Putative Kinase
Summary for 1KYH
Entry DOI | 10.2210/pdb1kyh/pdb |
Descriptor | Hypothetical 29.9 kDa protein in SIGY-CYDD intergenic region (2 entities in total) |
Functional Keywords | structural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function |
Biological source | Bacillus subtilis |
Total number of polymer chains | 1 |
Total formula weight | 30185.55 |
Authors | Zhang, R.,Dementieva, I.,Vinokour, E.,Collart, F.,Joachimiak, A.,Midwest Center for Structural Genomics (MCSG) (deposition date: 2002-02-04, release date: 2002-08-14, Last modification date: 2024-10-30) |
Primary citation | Zhang, R.,Grembecka, J.,Vinokour, E.,Collart, F.,Dementieva, I.,Minor, W.,Joachimiak, A. Structure of Bacillus subtilis YXKO--a member of the UPF0031 family and a putative kinase. J.Struct.Biol., 139:161-170, 2002 Cited by PubMed Abstract: 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. PubMed: 12457846DOI: 10.1016/S1047-8477(02)00532-4 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (1.6 Å) |
Structure validation
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