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1KYH

Structure of Bacillus subtilis YxkO, a Member of the UPF0031 Family and a Putative Kinase

Summary for 1KYH
Entry DOI10.2210/pdb1kyh/pdb
DescriptorHypothetical 29.9 kDa protein in SIGY-CYDD intergenic region (2 entities in total)
Functional Keywordsstructural genomics, psi, protein structure initiative, midwest center for structural genomics, mcsg, unknown function
Biological sourceBacillus subtilis
Total number of polymer chains1
Total formula weight30185.55
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 citationZhang, 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: 12457846
DOI: 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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數據於2024-11-06公開中

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