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PDBsum entry 2f5c
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Transcription
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PDB id
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2f5c
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Contents |
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* Residue conservation analysis
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DOI no:
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Biochemistry
45:3493-3505
(2006)
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PubMed id:
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Structural basis for the metal-selective activation of the manganese transport regulator of Bacillus subtilis.
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J.I.Kliegman,
S.L.Griner,
J.D.Helmann,
R.G.Brennan,
A.Glasfeld.
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ABSTRACT
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The manganese transport regulator (MntR) of Bacillus subtilis is activated by
Mn(2+) to repress transcription of genes encoding transporters involved in the
uptake of manganese. MntR is also strongly activated by cadmium, both in vivo
and in vitro, but it is poorly activated by other metal cations, including
calcium and zinc. The previously published MntR.Mn(2+) structure revealed a
binuclear complex of manganese ions with a metal-metal separation of 3.3 A
(herein designated the AB conformer). Analysis of four additional crystal forms
of MntR.Mn(2+) reveals that the AB conformer is only observed in monoclinic
crystals at 100 K, suggesting that this conformation may be stabilized by
crystal packing forces. In contrast, monoclinic crystals analyzed at room
temperature (at either pH 6.5 or pH 8.5), and a second hexagonal crystal form
(analyzed at 100 K), all reveal the shift of one manganese ion by 2.5 A, thereby
leading to a newly identified conformation (the AC conformer) with an
internuclear distance of 4.4 A. Significantly, the cadmium and calcium complexes
of MntR also contain binuclear complexes with a 4.4 A internuclear separation.
In contrast, the zinc complex of MntR contains only one metal ion per subunit,
in the A site. Isothermal titration calorimetry confirms the stoichiometry of
Mn(2+), Cd(2+), and Zn(2+) binding to MntR. We propose that the specificity of
MntR activation is tied to productive binding of metal ions at two sites; the A
site appears to act as a selectivity filter, determining whether the B or C site
will be occupied and thereby fully activate MntR.
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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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D.Osman,
and
J.S.Cavet
(2010).
Bacterial metal-sensing proteins exemplified by ArsR-SmtB family repressors.
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Nat Prod Rep,
27,
668-680.
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E.W.Moomaw,
A.Angerhofer,
P.Moussatche,
A.Ozarowski,
I.García-Rubio,
and
N.G.Richards
(2009).
Metal dependence of oxalate decarboxylase activity.
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Biochemistry,
48,
6116-6125.
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Z.Ma,
F.E.Jacobsen,
and
D.P.Giedroc
(2009).
Coordination chemistry of bacterial metal transport and sensing.
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Chem Rev,
109,
4644-4681.
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O.Okhrimenko,
and
I.Jelesarov
(2008).
A survey of the year 2006 literature on applications of isothermal titration calorimetry.
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J Mol Recognit,
21,
1.
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P.R.Chen,
and
C.He
(2008).
Selective recognition of metal ions by metalloregulatory proteins.
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Curr Opin Chem Biol,
12,
214-221.
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S.A.Shelburne,
D.B.Keith,
M.T.Davenport,
N.Horstmann,
R.G.Brennan,
and
J.M.Musser
(2008).
Molecular characterization of group A Streptococcus maltodextrin catabolism and its role in pharyngitis.
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Mol Microbiol,
69,
436-452.
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S.A.Shelburne,
D.Keith,
N.Horstmann,
P.Sumby,
M.T.Davenport,
E.A.Graviss,
R.G.Brennan,
and
J.M.Musser
(2008).
A direct link between carbohydrate utilization and virulence in the major human pathogen group A Streptococcus.
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Proc Natl Acad Sci U S A,
105,
1698-1703.
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T.G.Kloosterman,
R.M.Witwicki,
M.M.van der Kooi-Pol,
J.J.Bijlsma,
and
O.P.Kuipers
(2008).
Opposite effects of Mn2+ and Zn2+ on PsaR-mediated expression of the virulence genes pcpA, prtA, and psaBCA of Streptococcus pneumoniae.
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J Bacteriol,
190,
5382-5393.
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D.P.Giedroc,
and
A.I.Arunkumar
(2007).
Metal sensor proteins: nature's metalloregulated allosteric switches.
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Dalton Trans,
(),
3107-3120.
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M.A.DeWitt,
J.I.Kliegman,
J.D.Helmann,
R.G.Brennan,
D.L.Farrens,
and
A.Glasfeld
(2007).
The conformations of the manganese transport regulator of Bacillus subtilis in its metal-free state.
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J Mol Biol,
365,
1257-1265.
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PDB codes:
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M.Golynskiy,
S.Li,
V.L.Woods,
and
S.M.Cohen
(2007).
Conformational studies of the manganese transport regulator (MntR) from Bacillus subtilis using deuterium exchange mass spectrometry.
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J Biol Inorg Chem,
12,
699-709.
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N.Bhattacharya,
M.Yi,
H.X.Zhou,
and
T.M.Logan
(2007).
Backbone dynamics in an intramolecular prolylpeptide-SH3 complex from the diphtheria toxin repressor, DtxR.
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J Mol Biol,
374,
977-992.
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R.Thilakaraj,
K.Raghunathan,
S.Anishetty,
and
G.Pennathur
(2007).
In silico identification of putative metal binding motifs.
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Bioinformatics,
23,
267-271.
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J.W.Lee,
and
J.D.Helmann
(2006).
Biochemical characterization of the structural Zn2+ site in the Bacillus subtilis peroxide sensor PerR.
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J Biol Chem,
281,
23567-23578.
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M.V.Golynskiy,
W.A.Gunderson,
M.P.Hendrich,
and
S.M.Cohen
(2006).
Metal binding studies and EPR spectroscopy of the manganese transport regulator MntR.
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Biochemistry,
45,
15359-15372.
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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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Links
