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Structural genomics, unknown function
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PDB id
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1zyl
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Contents |
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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Cellular component
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cytoplasm
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1 term
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Biochemical function
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protein serine/threonine kinase activity
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1 term
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DOI no:
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Mol Microbiol
63:1360-1371
(2007)
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PubMed id:
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Crystal structure of a novel prokaryotic Ser/Thr kinase and its implication in the Cpx stress response pathway.
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J.Zheng,
C.He,
V.K.Singh,
N.L.Martin,
Z.Jia.
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ABSTRACT
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The Cpx signalling system of Escherichia coli and Salmonella enterica senses
extracytoplasmic stress and controls expression of factors that allow the
bacterium to adapt to these stressors and thereby enhance survival. Many of the
Cpx-responsive genes products are of unknown function. We determined the crystal
structure of one of these gene products, called YihE in E. coli, which exhibits
a eukaryotic kinase fold. Functional assays established that both YihE and the
S. enterica YihE homologue, RdoA, undergo autophosphorylation and phosphorylate
protein substrates at Ser/Thr residues in vitro, demonstrating that YihE/RdoA is
a novel Ser/Thr protein kinase in prokaryotic cells. Phenotypic analysis of
yihE/rdoA null strains indicates that this kinase is most abundant in stationary
phase, and is important for long-term cell survival and for expression of
surface appendages in both a Cpx-independent and -dependent manner. YihE/RdoA is
therefore a previously unknown kinase component of a new type of bacterial
phosphorelay mechanism, adding kinase activity as another response to the Cpx
sensing system that functions to maintain cellular homeostasis.
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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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A.Zorina,
N.Stepanchenko,
G.V.Novikova,
M.Sinetova,
V.B.Panichkin,
I.E.Moshkov,
V.V.Zinchenko,
S.V.Shestakov,
I.Suzuki,
N.Murata,
and
D.A.Los
(2011).
Eukaryotic-like Ser/Thr Protein Kinases SpkC/F/K Are Involved in Phosphorylation of GroES in the Cyanobacterium Synechocystis.
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DNA Res, 18,
137-151.
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N.Tyagi,
K.Anamika,
and
N.Srinivasan
(2010).
A framework for classification of prokaryotic protein kinases.
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PLoS One, 5,
e10608.
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A.J.Cozzone
(2009).
Bacterial tyrosine kinases: novel targets for antibacterial therapy?
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Trends Microbiol, 17,
536-543.
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E.Bechet,
S.Guiral,
S.Torres,
I.Mijakovic,
A.J.Cozzone,
and
C.Grangeasse
(2009).
Tyrosine-kinases in bacteria: from a matter of controversy to the status of key regulatory enzymes.
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Amino Acids, 37,
499-507.
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S.Lacour,
E.Bechet,
A.J.Cozzone,
I.Mijakovic,
and
C.Grangeasse
(2008).
Tyrosine phosphorylation of the UDP-glucose dehydrogenase of Escherichia coli is at the crossroads of colanic acid synthesis and polymyxin resistance.
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PLoS ONE, 3,
e3053.
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J.Marles-Wright,
and
R.J.Lewis
(2007).
Stress responses of bacteria.
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Curr Opin Struct Biol, 17,
755-760.
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N.L.Martin
(2007).
Sequence plus structure plus experimental inquiry: combining the clues to elucidate bacterial kinase function.
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Future Microbiol, 2,
223-226.
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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.
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Links
