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Transcription
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PDB id
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1lj9
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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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intracellular
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1 term
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Biological process
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transcription, DNA-dependent
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2 terms
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Biochemical function
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DNA binding
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2 terms
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DOI no:
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J Biol Chem
278:20240-20244
(2003)
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PubMed id:
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Crystal structure of Enterococcus faecalis SlyA-like transcriptional factor.
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R.Y.Wu,
R.G.Zhang,
O.Zagnitko,
I.Dementieva,
N.Maltzev,
J.D.Watson,
R.Laskowski,
P.Gornicki,
A.Joachimiak.
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ABSTRACT
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The crystal structure of a SlyA transcriptional regulator at 1.6 A resolution is
presented, and structural relationships between members of the MarR/SlyA family
are discussed. The SlyA family, which includes SlyA, Rap, Hor, and RovA
proteins, is widely distributed in bacterial and archaeal genomes. Current
evidence suggests that SlyA-like factors act as repressors, activators, and
modulators of gene transcription. These proteins have been shown to up-regulate
the expression of molecular chaperones, acid-resistance proteins, and cytolysin,
and down-regulate several biosynthetic enzymes. The structure of SlyA from
Enterococcus faecalis, determined as a part of an ongoing structural genomics
initiative (www.mcsg.anl.gov), revealed the same winged helix DNA-binding motif
that was recently found in the MarR repressor from Escherichia coli and the MexR
repressor from Pseudomonas aeruginosa, a sequence homologue of MarR.
Phylogenetic analysis of the MarR/SlyA family suggests that Sly is placed
between the SlyA and MarR subfamilies and shows significant sequence similarity
to members of both subfamilies.
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Selected figure(s)
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Figure 3.
FIG. 3. Secondary and domain structure of SlyA-Ef. A,
secondary structure of SlyA-Ef. b, SlyA-Ef dimerization domain
showing domain swapping. c, DNA-binding domain with winged helix
motif. Drawings prepared with WebLabViewerPro.
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Figure 4.
FIG. 4. Comparison of the SlyA-Ef structure with the
structures of MarR and MexR. a, superimposition of SlyA-Ef
(blue) on MarR (red) subunits. b, superimposition of the SlyA-Ef
(blue) and MexR (red) structures.
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The above figures are
reprinted
by permission from the ASBMB:
J Biol Chem
(2003,
278,
20240-20244)
copyright 2003.
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Figures were
selected
by an automated process.
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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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B.Apostolovic,
M.Danial,
and
H.A.Klok
(2010).
Coiled coils: attractive protein folding motifs for the fabrication of self-assembled, responsive and bioactive materials.
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Chem Soc Rev, 39,
3541-3575.
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C.Andrésen,
S.Jalal,
D.Aili,
Y.Wang,
S.Islam,
A.Jarl,
B.Liedberg,
B.Wretlind,
L.G.Mårtensson,
and
M.Sunnerhagen
(2010).
Critical biophysical properties in the Pseudomonas aeruginosa efflux gene regulator MexR are targeted by mutations conferring multidrug resistance.
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| |
Protein Sci, 19,
680-692.
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|
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V.Duarte,
and
J.M.Latour
(2010).
PerR vs OhrR: selective peroxide sensing in Bacillus subtilis.
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| |
Mol Biosyst, 6,
316-323.
|
 |
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|
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Y.M.Chang,
W.Y.Jeng,
T.P.Ko,
Y.J.Yeh,
C.K.Chen,
and
A.H.Wang
(2010).
Structural study of TcaR and its complexes with multiple antibiotics from Staphylococcus epidermidis.
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Proc Natl Acad Sci U S A, 107,
8617-8622.
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PDB codes:
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C.E.Nichols,
S.Sainsbury,
J.Ren,
T.S.Walter,
A.Verma,
D.K.Stammers,
N.J.Saunders,
and
R.J.Owens
(2009).
The structure of NMB1585, a MarR-family regulator from Neisseria meningitidis.
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun, 65,
204-209.
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PDB code:
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P.Xue,
D.Corbett,
M.Goldrick,
C.Naylor,
and
I.S.Roberts
(2009).
Regulation of expression of the region 3 promoter of the Escherichia coli K5 capsule gene cluster involves H-NS, SlyA, and a large 5' untranslated region.
|
| |
J Bacteriol, 191,
1838-1846.
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T.Kumarevel,
T.Tanaka,
T.Umehara,
and
S.Yokoyama
(2009).
ST1710-DNA complex crystal structure reveals the DNA binding mechanism of the MarR family of regulators.
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Nucleic Acids Res, 37,
4723-4735.
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PDB codes:
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E.A.Sieminska,
X.Xu,
A.Savchenko,
and
D.A.Sanders
(2007).
The X-ray crystal structure of PA1607 from Pseudomonas aureginosa at 1.9 A resolution--a putative transcription factor.
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Protein Sci, 16,
543-549.
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PDB code:
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J.K.Lithgow,
F.Haider,
I.S.Roberts,
and
J.Green
(2007).
Alternate SlyA and H-NS nucleoprotein complexes control hlyE expression in Escherichia coli K-12.
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| |
Mol Microbiol, 66,
685-698.
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K.J.Newberry,
M.Fuangthong,
W.Panmanee,
S.Mongkolsuk,
and
R.G.Brennan
(2007).
Structural mechanism of organic hydroperoxide induction of the transcription regulator OhrR.
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Mol Cell, 28,
652-664.
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PDB codes:
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D.W.Ellison,
and
V.L.Miller
(2006).
Regulation of virulence by members of the MarR/SlyA family.
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| |
Curr Opin Microbiol, 9,
153-159.
|
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|
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K.H.Chin,
Z.L.Tu,
J.N.Li,
C.C.Chou,
A.H.Wang,
and
S.H.Chou
(2006).
The crystal structure of XC1739: a putative multiple antibiotic-resistance repressor (MarR) from Xanthomonas campestris at 1.8 A resolution.
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Proteins, 65,
239-242.
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PDB code:
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W.Panmanee,
P.Vattanaviboon,
L.B.Poole,
and
S.Mongkolsuk
(2006).
Novel organic hydroperoxide-sensing and responding mechanisms for OhrR, a major bacterial sensor and regulator of organic hydroperoxide stress.
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| |
J Bacteriol, 188,
1389-1395.
|
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|
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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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|
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M.Hong,
M.Fuangthong,
J.D.Helmann,
and
R.G.Brennan
(2005).
Structure of an OhrR-ohrA operator complex reveals the DNA binding mechanism of the MarR family.
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| |
Mol Cell, 20,
131-141.
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PDB codes:
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M.J.Ferrándiz,
K.Bishop,
P.Williams,
and
H.Withers
(2005).
HosA, a member of the SlyA family, regulates motility in enteropathogenic Escherichia coli.
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| |
Infect Immun, 73,
1684-1694.
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|
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R.S.De Silva,
G.Kovacikova,
W.Lin,
R.K.Taylor,
K.Skorupski,
and
F.J.Kull
(2005).
Crystal structure of the virulence gene activator AphA from Vibrio cholerae reveals it is a novel member of the winged helix transcription factor superfamily.
|
| |
J Biol Chem, 280,
13779-13783.
|
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PDB code:
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|
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W.W.Navarre,
T.A.Halsey,
D.Walthers,
J.Frye,
M.McClelland,
J.L.Potter,
L.J.Kenney,
J.S.Gunn,
F.C.Fang,
and
S.J.Libby
(2005).
Co-regulation of Salmonella enterica genes required for virulence and resistance to antimicrobial peptides by SlyA and PhoP/PhoQ.
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| |
Mol Microbiol, 56,
492-508.
|
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|
|
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|
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D.Tropel,
and
J.R.van der Meer
(2004).
Bacterial transcriptional regulators for degradation pathways of aromatic compounds.
|
| |
Microbiol Mol Biol Rev, 68,
474-500.
|
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|
|
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|
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G.Kovacikova,
W.Lin,
and
K.Skorupski
(2004).
Vibrio cholerae AphA uses a novel mechanism for virulence gene activation that involves interaction with the LysR-type regulator AphB at the tcpPH promoter.
|
| |
Mol Microbiol, 53,
129-142.
|
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|
|
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|
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M.A.Prieto,
B.Galán,
B.Torres,
A.Ferrández,
C.Fernández,
B.Miñambres,
J.L.García,
and
E.Díaz
(2004).
Aromatic metabolism versus carbon availability: the regulatory network that controls catabolism of less-preferred carbon sources in Escherichia coli.
|
| |
FEMS Microbiol Rev, 28,
503-518.
|
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|
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|
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N.R.Wyborn,
M.R.Stapleton,
V.A.Norte,
R.E.Roberts,
J.Grafton,
and
J.Green
(2004).
Regulation of Escherichia coli hemolysin E expression by H-NS and Salmonella SlyA.
|
| |
J Bacteriol, 186,
1620-1628.
|
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|
|
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|
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P.Kraft,
A.Oeckinghaus,
D.Kümmel,
G.H.Gauss,
J.Gilmore,
B.Wiedenheft,
M.Young,
and
C.M.Lawrence
(2004).
Crystal structure of F-93 from Sulfolobus spindle-shaped virus 1, a winged-helix DNA binding protein.
|
| |
J Virol, 78,
11544-11550.
|
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|
PDB code:
|
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|
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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.
|
| |
J Struct Funct Genomics, 5,
111-118.
|
 |
|
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|
|
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B.Galán,
A.Kolb,
J.M.Sanz,
J.L.García,
and
M.A.Prieto
(2003).
Molecular determinants of the hpa regulatory system of Escherichia coli: the HpaR repressor.
|
| |
Nucleic Acids Res, 31,
6598-6609.
|
 |
|
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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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