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PDBsum entry 2di3
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Transcription
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PDB id
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2di3
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Contents |
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* Residue conservation analysis
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Nucleic Acids Res
36:7110-7123
(2008)
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PubMed id:
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Structural and functional characterization of the LldR from Corynebacterium glutamicum: a transcriptional repressor involved in L-lactate and sugar utilization.
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Y.G.Gao,
H.Suzuki,
H.Itou,
Y.Zhou,
Y.Tanaka,
M.Wachi,
N.Watanabe,
I.Tanaka,
M.Yao.
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ABSTRACT
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LldR (CGL2915) from Corynebacterium glutamicum is a transcription factor
belonging to the GntR family, which is typically involved in the regulation of
oxidized substrates associated with amino acid metabolism. In the present study,
the crystal structure of LldR was determined at 2.05-A resolution. The structure
consists of N- and C-domains similar to those of FadR, but with distinct domain
orientations. LldR and FadR dimers achieve similar structures by domain
swapping, which was first observed in dimeric assembly of transcription factors.
A structural feature of Zn(2+) binding in the regulatory domain was also
observed, as a difference from the FadR subfamily. DNA microarray and DNase I
footprint analyses suggested that LldR acts as a repressor regulating
cgl2917-lldD and cgl1934-fruK-ptsF operons, which are indispensable for
l-lactate and fructose/sucrose utilization, respectively. Furthermore, the
stoichiometries and affinities of LldR and DNAs were determined by isothermal
titration calorimetry measurements. The transcriptional start site and
repression of LldR on the cgl2917-lldD operon were analysed by primer extension
assay. Mutation experiments showed that residues Lys4, Arg32, Arg42 and Gly63
are crucial for DNA binding. The location of the putative ligand binding cavity
and the regulatory mechanism of LldR on its affinity for DNA were proposed.
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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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H.Teramoto,
M.Inui,
and
H.Yukawa
(2010).
Regulation of genes involved in sugar uptake, glycolysis and lactate production in Corynebacterium glutamicum.
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Future Microbiol,
5,
1475-1481.
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O.Kato,
J.W.Youn,
K.C.Stansen,
D.Matsui,
T.Oikawa,
and
V.F.Wendisch
(2010).
Quinone-dependent D-lactate dehydrogenase Dld (Cg1027) is essential for growth of Corynebacterium glutamicum on D-lactate.
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BMC Microbiol,
10,
321.
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R.J.Falconer,
A.Penkova,
I.Jelesarov,
and
B.M.Collins
(2010).
Survey of the year 2008: applications of isothermal titration calorimetry.
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J Mol Recognit,
23,
395-413.
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K.Toyoda,
H.Teramoto,
M.Inui,
and
H.Yukawa
(2009).
The ldhA gene, encoding fermentative L-lactate dehydrogenase of Corynebacterium glutamicum, is under the control of positive feedback regulation mediated by LldR.
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J Bacteriol,
191,
4251-4258.
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M.Zheng,
D.R.Cooper,
N.E.Grossoehme,
M.Yu,
L.W.Hung,
M.Cieslik,
U.Derewenda,
S.A.Lesley,
I.A.Wilson,
D.P.Giedroc,
and
Z.S.Derewenda
(2009).
Structure of Thermotoga maritima TM0439: implications for the mechanism of bacterial GntR transcription regulators with Zn(2+)-binding FCD domains.
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Acta Crystallogr D Biol Crystallogr,
65,
356-365.
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PDB code:
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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
code is
shown on the right.
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Links
