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* Residue conservation analysis
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Gene Ontology (GO) functional annotation
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Biochemical function
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protein binding
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1 term
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DOI no:
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J Bacteriol
190:6795-6804
(2008)
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PubMed id:
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O2- and NO-sensing mechanism through the DevSR two-component system in Mycobacterium smegmatis.
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J.M.Lee,
H.Y.Cho,
H.J.Cho,
I.J.Ko,
S.W.Park,
H.S.Baik,
J.H.Oh,
C.Y.Eom,
Y.M.Kim,
B.S.Kang,
J.I.Oh.
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ABSTRACT
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The DevS histidine kinase of Mycobacterium smegmatis contains tandem GAF domains
(GAF-A and GAF-B) in its N-terminal sensory domain. The heme iron of DevS is in
the ferrous state when purified and is resistant to autooxidation from a ferrous
to a ferric state in the presence of O(2). The redox property of the heme and
the results of sequence comparison analysis indicate that DevS of M. smegmatis
is more closely related to DosT of Mycobacterium tuberculosis than DevS of M.
tuberculosis. The binding of O(2) to the deoxyferrous heme led to a decrease in
the autokinase activity of DevS, whereas NO binding did not. The regulation of
DevS autokinase activity in response to O(2) and NO was not observed in the DevS
derivatives lacking its heme, indicating that the ligand-binding state of the
heme plays an important role in the regulation of DevS kinase activity. The
redox state of the quinone/quinol pool of the respiratory electron transport
chain appears not to be implicated in the regulation of DevS activity. Neither
cyclic GMP (cGMP) nor cAMP affected DevS autokinase activity, excluding the
possibility that the cyclic nucleotides serve as the effector molecules to
modulate DevS kinase activity. The three-dimensional structure of the putative
GAF-B domain revealed that it has a GAF folding structure without cyclic
nucleotide binding capacity.
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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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J.Cheung,
and
W.A.Hendrickson
(2010).
Sensor domains of two-component regulatory systems.
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Curr Opin Microbiol, 13,
116-123.
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M.J.Kim,
K.J.Park,
I.J.Ko,
Y.M.Kim,
and
J.I.Oh
(2010).
Different roles of DosS and DosT in the hypoxic adaptation of Mycobacteria.
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J Bacteriol, 192,
4868-4875.
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N.K.Taneja,
S.Dhingra,
A.Mittal,
M.Naresh,
and
J.S.Tyagi
(2010).
Mycobacterium tuberculosis transcriptional adaptation, growth arrest and dormancy phenotype development is triggered by vitamin C.
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PLoS One, 5,
e10860.
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B.A.Roxas,
and
Q.Li
(2009).
Acid stress response of a mycobacterial proteome: insight from a gene ontology analysis.
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Int J Clin Exp Med, 2,
309-328.
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H.Y.Cho,
H.J.Cho,
Y.M.Kim,
J.I.Oh,
and
B.S.Kang
(2009).
Structural insight into the heme-based redox sensing by DosS from Mycobacterium tuberculosis.
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J Biol Chem, 284,
13057-13067.
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PDB codes:
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J.Green,
J.C.Crack,
A.J.Thomson,
and
N.E.LeBrun
(2009).
Bacterial sensors of oxygen.
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Curr Opin Microbiol, 12,
145-151.
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R.Gao,
and
A.M.Stock
(2009).
Biological insights from structures of two-component proteins.
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Annu Rev Microbiol, 63,
133-154.
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R.W.Honaker,
R.L.Leistikow,
I.L.Bartek,
and
M.I.Voskuil
(2009).
Unique roles of DosT and DosS in DosR regulon induction and Mycobacterium tuberculosis dormancy.
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Infect Immun, 77,
3258-3263.
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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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