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PDBsum entry 1kyh
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Structural genomics, unknown function
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PDB id
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1kyh
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Contents |
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* Residue conservation analysis
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Enzyme class:
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E.C.4.2.1.136
- ADP-dependent NAD(P)H-hydrate dehydratase.
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Reaction:
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1.
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(6S)-NADHX + ADP = AMP + phosphate + NADH + H+
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2.
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(6S)-NADPHX + ADP = AMP + phosphate + NADPH + H+
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(6S)-NADHX
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+
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ADP
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=
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AMP
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+
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phosphate
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+
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NADH
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+
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H(+)
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(6S)-NADPHX
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+
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ADP
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=
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AMP
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+
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phosphate
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+
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NADPH
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+
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H(+)
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Molecule diagrams generated from .mol files obtained from the
KEGG ftp site
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DOI no:
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J Struct Biol
139:161-170
(2002)
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PubMed id:
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Structure of Bacillus subtilis YXKO--a member of the UPF0031 family and a putative kinase.
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R.G.Zhang,
J.Grembecka,
E.Vinokour,
F.Collart,
I.Dementieva,
W.Minor,
A.Joachimiak.
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ABSTRACT
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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.
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Literature references that cite this PDB file's key reference
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PubMed id
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Reference
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Y.F.Zhou,
L.F.Li,
C.Yang,
Y.H.Liang,
and
X.D.Su
(2008).
Preliminary X-ray crystallographic analysis of SMU.573, a putative sugar kinase from Streptococcus mutans.
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Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
47-49.
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D.Ulanova,
V.Holanová,
L.Prenosilová,
J.Náprstek,
and
I.Lichá
(2007).
Mutation of a gene encoding a putative ribokinase leads to reduced salt tolerance under potassium limitation in Bacillus subtilis.
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Folia Microbiol (Praha),
52,
203-208.
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Y.Zhang,
M.H.El Kouni,
and
S.E.Ealick
(2007).
Substrate analogs induce an intermediate conformational change in Toxoplasma gondii adenosine kinase.
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Acta Crystallogr D Biol Crystallogr,
63,
126-134.
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PDB codes:
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L.Arnfors,
T.Hansen,
P.Schönheit,
R.Ladenstein,
and
W.Meining
(2006).
Structure of Methanocaldococcus jannaschii nucleoside kinase: an archaeal member of the ribokinase family.
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Acta Crystallogr D Biol Crystallogr,
62,
1085-1097.
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PDB codes:
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Y.Qiu,
V.Tereshko,
Y.Kim,
R.Zhang,
F.Collart,
M.Yousef,
A.Kossiakoff,
and
A.Joachimiak
(2006).
The crystal structure of Aq_328 from the hyperthermophilic bacteria Aquifex aeolicus shows an ancestral histone fold.
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Proteins,
62,
8.
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PDB code:
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Y.Zhang,
M.H.El Kouni,
and
S.E.Ealick
(2006).
Structure of Toxoplasma gondii adenosine kinase in complex with an ATP analog at 1.1 angstroms resolution.
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Acta Crystallogr D Biol Crystallogr,
62,
140-145.
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PDB code:
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B.Nocek,
C.Chang,
H.Li,
L.Lezondra,
D.Holzle,
F.Collart,
and
A.Joachimiak
(2005).
Crystal structures of delta1-pyrroline-5-carboxylate reductase from human pathogens Neisseria meningitides and Streptococcus pyogenes.
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J Mol Biol,
354,
91.
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PDB codes:
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F.J.Stevens,
C.Kuemmel,
G.Babnigg,
and
F.R.Collart
(2005).
Efficient recognition of protein fold at low sequence identity by conservative application of Psi-BLAST: application.
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J Mol Recognit,
18,
150-157.
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Y.Kim,
I.Dementieva,
M.Zhou,
R.Wu,
L.Lezondra,
P.Quartey,
G.Joachimiak,
O.Korolev,
H.Li,
and
A.Joachimiak
(2004).
Automation of protein purification for structural genomics.
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J Struct Funct Genomics,
5,
111-118.
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The most recent references are shown first.
Citation data come partly from CiteXplore and partly
from an automated harvesting procedure. Note that this is likely to be
only a partial list as not all journals are covered by
either method. However, we are continually building up the citation data
so more and more references will be included with time.
Where a reference describes a PDB structure, the PDB
codes are
shown on the right.
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}
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