 |
PDBsum entry 1kyh
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
 |
|
|
|
|
|
|
|
|
|
|
Structural genomics, unknown function
|
PDB id
|
|
|
|
1kyh
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
References listed in PDB file
|
 |
|
Key reference
|
 |
|
Title
|
 |
Structure of bacillus subtilis yxko--A member of the upf0031 family and a putative kinase.
|
 |
|
Authors
|
 |
R.G.Zhang,
J.Grembecka,
E.Vinokour,
F.Collart,
I.Dementieva,
W.Minor,
A.Joachimiak.
|
 |
|
Ref.
|
 |
J Struct Biol, 2002,
139,
161-170.
[DOI no: ]
|
 |
|
PubMed id
|
 |
|
 |
 |
|
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.
|
 |
|
|
|
|
 |