 |
PDBsum entry 1gxq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
Transcriptional activator
|
PDB id
|
|
|
|
1gxq
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
Contents |
 |
|
|
|
|
|
|
|
|
|
|
* Residue conservation analysis
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
|
|
|
|
|
|
| |
|
DOI no:
|
Structure
10:701-713
(2002)
|
|
PubMed id:
|
|
|
|
|
|
| |
|
Tandem DNA recognition by PhoB, a two-component signal transduction transcriptional activator.
|
|
A.G.Blanco,
M.Sola,
F.X.Gomis-Rüth,
M.Coll.
|
|
|
|
|
| |
ABSTRACT
|
|
|
|
| |
|
|
PhoB is a signal transduction response regulator that activates nearly 40 genes
in phosphate depletion conditions in E. coli and closely related bacteria. The
structure of the PhoB effector domain in complex with its target DNA sequence,
or pho box, reveals a novel tandem arrangement in which several monomers bind
head to tail to successive 11-base pair direct-repeat sequences, coating one
face of a smoothly bent double helix. The protein has a winged helix fold in
which the DNA recognition elements comprise helix alpha 3, penetrating the major
groove, and a beta hairpin wing interacting with a compressed minor groove via
Arg219, tightly sandwiched between the DNA sugar backbones. The transactivation
loops protrude laterally in an appropriate orientation to interact with the RNA
polymerase sigma(70) subunit, which triggers transcription initiation.
|
|
|
|
|
|
| |
Selected figure(s)
|
|
|
|
| |
|
|
|
|
Figure 6.
Figure 6. Proposed Mechanism of InhibitionSuperposition of
two full-length DrrD molecules (pink and green) with two PhoB^RD
and two PhoB^DBTD bound to DNA (colored as in Figure 2B) showing
steric clashes between adjacent monomers.
|
|
|
|
|
|
| |
The above figure is
reprinted
by permission from Cell Press:
Structure
(2002,
10,
701-713)
copyright 2002.
|
|
| |
Figure was
selected
by an automated process.
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
|
 |
 |
 |
|
Literature references that cite this PDB file's key reference
|
|
|
| |
PubMed id
|
|
Reference
|
|
|
|
|
|
A.Doi,
T.Okajima,
Y.Gotoh,
K.Tanizawa,
and
R.Utsumi
(2010).
X-ray crystal structure of the DNA-binding domain of response regulator WalR essential to the cell viability of staphylococcus aureus and interaction with target DNA.
|
| |
Biosci Biotechnol Biochem,
74,
1901-1907.
|
|
|
|
|
|
|
M.L.López-Redondo,
F.Moronta,
P.Salinas,
J.Espinosa,
R.Cantos,
R.Dixon,
A.Marina,
and
A.Contreras
(2010).
Environmental control of phosphorylation pathways in a branched two-component system.
|
| |
Mol Microbiol,
78,
475-489.
|
|
|
|
|
|
|
M.Y.Galperin
(2010).
Diversity of structure and function of response regulator output domains.
|
| |
Curr Opin Microbiol,
13,
150-159.
|
|
|
|
|
|
|
O.Harari,
S.Y.Park,
H.Huang,
E.A.Groisman,
and
I.Zwir
(2010).
Defining the plasticity of transcription factor binding sites by Deconstructing DNA consensus sequences: the PhoP-binding sites among gamma/enterobacteria.
|
| |
PLoS Comput Biol,
6,
e1000862.
|
|
|
|
|
|
|
Y.J.Hsieh,
and
B.L.Wanner
(2010).
Global regulation by the seven-component Pi signaling system.
|
| |
Curr Opin Microbiol,
13,
198-203.
|
|
|
|
|
|
|
A.Rodríguez-García,
A.Sola-Landa,
K.Apel,
F.Santos-Beneit,
and
J.F.Martín
(2009).
Phosphate control over nitrogen metabolism in Streptomyces coelicolor: direct and indirect negative control of glnR, glnA, glnII and amtB expression by the response regulator PhoP.
|
| |
Nucleic Acids Res,
37,
3230-3242.
|
|
|
|
|
|
|
C.Cheng,
S.M.Tennant,
K.I.Azzopardi,
V.Bennett-Wood,
E.L.Hartland,
R.M.Robins-Browne,
and
M.Tauschek
(2009).
Contribution of the pst-phoU operon to cell adherence by atypical enteropathogenic Escherichia coli and virulence of Citrobacter rodentium.
|
| |
Infect Immun,
77,
1936-1944.
|
|
|
|
|
|
|
C.Yanover,
M.Singh,
and
E.Zaslavsky
(2009).
M are better than one: an ensemble-based motif finder and its application to regulatory element prediction.
|
| |
Bioinformatics,
25,
868-874.
|
|
|
|
|
|
|
J.C.Perez,
and
E.A.Groisman
(2009).
Evolution of transcriptional regulatory circuits in bacteria.
|
| |
Cell,
138,
233-244.
|
|
|
|
|
|
|
K.Herz,
A.Rimon,
G.Jeschke,
and
E.Padan
(2009).
{beta}-Sheet-dependent Dimerization Is Essential for the Stability of NhaA Na+/H+ Antiporter.
|
| |
J Biol Chem,
284,
6337-6347.
|
|
|
|
|
|
|
K.Wollschläger,
K.Gaus,
A.Körnig,
R.Eckel,
S.D.Wilking,
M.McIntosh,
Z.Majer,
A.Becker,
R.Ros,
D.Anselmetti,
and
N.Sewald
(2009).
Single-molecule experiments to elucidate the minimal requirement for DNA recognition by transcription factor epitopes.
|
| |
Small,
5,
484-495.
|
|
|
|
|
|
|
M.McIntosh,
S.Meyer,
and
A.Becker
(2009).
Novel Sinorhizobium meliloti quorum sensing positive and negative regulatory feedback mechanisms respond to phosphate availability.
|
| |
Mol Microbiol,
74,
1238-1256.
|
|
|
|
|
|
|
M.S.Antunes,
K.J.Morey,
N.Tewari-Singh,
T.A.Bowen,
J.J.Smith,
C.T.Webb,
H.W.Hellinga,
and
J.I.Medford
(2009).
Engineering key components in a synthetic eukaryotic signal transduction pathway.
|
| |
Mol Syst Biol,
5,
270.
|
|
|
|
|
|
|
M.Varedian,
M.Erdélyi,
A.Persson,
and
A.Gogoll
(2009).
Interplaying factors for the formation of photoswitchable beta-hairpins: the advantage of a flexible switch.
|
| |
J Pept Sci,
15,
107-113.
|
|
|
|
|
|
|
S.Gupta,
A.Pathak,
A.Sinha,
and
D.Sarkar
(2009).
Mycobacterium tuberculosis PhoP recognizes two adjacent direct-repeat sequences to form head-to-head dimers.
|
| |
J Bacteriol,
191,
7466-7476.
|
|
|
|
|
|
|
S.S.Gupta,
B.N.Borin,
T.L.Cover,
and
A.M.Krezel
(2009).
Structural Analysis of the DNA-binding Domain of the Helicobacter pylori Response Regulator ArsR.
|
| |
J Biol Chem,
284,
6536-6545.
|
|
|
|
|
|
|
T.R.Mack,
R.Gao,
and
A.M.Stock
(2009).
Probing the roles of the two different dimers mediated by the receiver domain of the response regulator PhoB.
|
| |
J Mol Biol,
389,
349-364.
|
|
|
|
|
|
|
A.Sola-Landa,
A.Rodríguez-García,
A.K.Apel,
and
J.F.Martín
(2008).
Target genes and structure of the direct repeats in the DNA-binding sequences of the response regulator PhoP in Streptomyces coelicolor.
|
| |
Nucleic Acids Res,
36,
1358-1368.
|
|
|
|
|
|
|
C.Bahlawane,
B.Baumgarth,
J.Serrania,
S.Rüberg,
and
A.Becker
(2008).
Fine-tuning of galactoglucan biosynthesis in Sinorhizobium meliloti by differential WggR (ExpG)-, PhoB-, and MucR-dependent regulation of two promoters.
|
| |
J Bacteriol,
190,
3456-3466.
|
|
|
|
|
|
|
I.Lozada-Chávez,
V.E.Angarica,
J.Collado-Vides,
and
B.Contreras-Moreira
(2008).
The role of DNA-binding specificity in the evolution of bacterial regulatory networks.
|
| |
J Mol Biol,
379,
627-643.
|
|
|
|
|
|
|
J.Gonzalo-Asensio,
C.Y.Soto,
A.Arbués,
J.Sancho,
M.del Carmen Menéndez,
M.J.García,
B.Gicquel,
and
C.Martín
(2008).
The Mycobacterium tuberculosis phoPR operon is positively autoregulated in the virulent strain H37Rv.
|
| |
J Bacteriol,
190,
7068-7078.
|
|
|
|
|
|
|
L.Li,
R.M.Alvey,
R.P.Bezy,
and
D.M.Kehoe
(2008).
Inverse transcriptional activities during complementary chromatic adaptation are controlled by the response regulator RcaC binding to red and green light-responsive promoters.
|
| |
Mol Microbiol,
68,
286-297.
|
|
|
|
|
|
|
M.G.Lamarche,
B.L.Wanner,
S.Crépin,
and
J.Harel
(2008).
The phosphate regulon and bacterial virulence: a regulatory network connecting phosphate homeostasis and pathogenesis.
|
| |
FEMS Microbiol Rev,
32,
461-473.
|
|
|
|
|
|
|
M.L.Chesne-Seck,
N.Barilone,
F.Boudou,
J.Gonzalo Asensio,
P.E.Kolattukudy,
C.Martín,
S.T.Cole,
B.Gicquel,
D.N.Gopaul,
and
M.Jackson
(2008).
A point mutation in the two-component regulator PhoP-PhoR accounts for the absence of polyketide-derived acyltrehaloses but not that of phthiocerol dimycocerosates in Mycobacterium tuberculosis H37Ra.
|
| |
J Bacteriol,
190,
1329-1334.
|
|
|
|
|
|
|
M.McIntosh,
E.Krol,
and
A.Becker
(2008).
Competitive and cooperative effects in quorum-sensing-regulated galactoglucan biosynthesis in Sinorhizobium meliloti.
|
| |
J Bacteriol,
190,
5308-5317.
|
|
|
|
|
|
|
M.de Been,
M.J.Bart,
T.Abee,
R.J.Siezen,
and
C.Francke
(2008).
The identification of response regulator-specific binding sites reveals new roles of two-component systems in Bacillus cereus and closely related low-GC Gram-positives.
|
| |
Environ Microbiol,
10,
2796-2809.
|
|
|
|
|
|
|
R.A.Daly,
and
C.P.Lostroh
(2008).
Genetic analysis of the Salmonella transcription factor HilA.
|
| |
Can J Microbiol,
54,
854-860.
|
|
|
|
|
|
|
S.Crepin,
M.G.Lamarche,
P.Garneau,
J.Seguin,
J.Proulx,
C.M.Dozois,
and
J.Harel
(2008).
Genome-wide transcriptional response of an avian pathogenic Escherichia coli (APEC) pst mutant.
|
| |
BMC Genomics,
9,
568.
|
|
|
|
|
|
|
S.J.Cariss,
A.E.Tayler,
and
M.B.Avison
(2008).
Defining the growth conditions and promoter-proximal DNA sequences required for activation of gene expression by CreBC in Escherichia coli.
|
| |
J Bacteriol,
190,
3930-3939.
|
|
|
|
|
|
|
S.Wang,
Y.X.He,
R.Bao,
Y.B.Teng,
B.P.Ye,
and
C.Z.Zhou
(2008).
Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of hypothetical protein SCO4226 from Streptomyces coelicolor A3(2).
|
| |
Acta Crystallogr Sect F Struct Biol Cryst Commun,
64,
847-850.
|
|
|
|
|
|
|
T.Yamane,
H.Okamura,
M.Ikeguchi,
Y.Nishimura,
and
A.Kidera
(2008).
Water-mediated interactions between DNA and PhoB DNA-binding/transactivation domain: NMR-restrained molecular dynamics in explicit water environment.
|
| |
Proteins,
71,
1970-1983.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
C.H.Trinh,
Y.Liu,
S.E.Phillips,
and
M.K.Phillips-Jones
(2007).
Structure of the response regulator VicR DNA-binding domain.
|
| |
Acta Crystallogr D Biol Crystallogr,
63,
266-269.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
D.L.Stauff,
V.J.Torres,
and
E.P.Skaar
(2007).
Signaling and DNA-binding activities of the Staphylococcus aureus HssR-HssS two-component system required for heme sensing.
|
| |
J Biol Chem,
282,
26111-26121.
|
|
|
|
|
|
|
E.Hong,
H.M.Lee,
H.Ko,
D.U.Kim,
B.Y.Jeon,
J.Jung,
J.Shin,
S.A.Lee,
Y.Kim,
Y.H.Jeon,
C.Cheong,
H.S.Cho,
and
W.Lee
(2007).
Structure of an atypical orphan response regulator protein supports a new phosphorylation-independent regulatory mechanism.
|
| |
J Biol Chem,
282,
20667-20675.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
G.Churchward
(2007).
The two faces of Janus: virulence gene regulation by CovR/S in group A streptococci.
|
| |
Mol Microbiol,
64,
34-41.
|
|
|
|
|
|
|
J.King-Scott,
E.Nowak,
E.Mylonas,
S.Panjikar,
M.Roessle,
D.I.Svergun,
and
P.A.Tucker
(2007).
The structure of a full-length response regulator from Mycobacterium tuberculosis in a stabilized three-dimensional domain-swapped, activated state.
|
| |
J Biol Chem,
282,
37717-37729.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
N.Friedland,
T.R.Mack,
M.Yu,
L.W.Hung,
T.C.Terwilliger,
G.S.Waldo,
and
A.M.Stock
(2007).
Domain orientation in the inactive response regulator Mycobacterium tuberculosis MtrA provides a barrier to activation.
|
| |
Biochemistry,
46,
6733-6743.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
R.Arribas-Bosacoma,
S.K.Kim,
C.Ferrer-Orta,
A.G.Blanco,
P.J.Pereira,
F.X.Gomis-Rüth,
B.L.Wanner,
M.Coll,
and
M.Solà
(2007).
The X-ray crystal structures of two constitutively active mutants of the Escherichia coli PhoB receiver domain give insights into activation.
|
| |
J Mol Biol,
366,
626-641.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
S.Wang,
J.Engohang-Ndong,
and
I.Smith
(2007).
Structure of the DNA-binding domain of the response regulator PhoP from Mycobacterium tuberculosis.
|
| |
Biochemistry,
46,
14751-14761.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
W.Juntarajumnong,
T.A.Hirani,
J.M.Simpson,
A.Incharoensakdi,
and
J.J.Eaton-Rye
(2007).
Phosphate sensing in Synechocystis sp. PCC 6803: SphU and the SphS-SphR two-component regulatory system.
|
| |
Arch Microbiol,
188,
389-402.
|
|
|
|
|
|
|
Z.Su,
V.Olman,
and
Y.Xu
(2007).
Computational prediction of Pho regulons in cyanobacteria.
|
| |
BMC Genomics,
8,
156.
|
|
|
|
|
|
|
C.Laguri,
R.A.Stenzel,
T.J.Donohue,
M.K.Phillips-Jones,
and
M.P.Williamson
(2006).
Activation of the global gene regulator PrrA (RegA) from Rhodobacter sphaeroides.
|
| |
Biochemistry,
45,
7872-7881.
|
|
|
|
|
|
|
K.Yamamoto,
and
A.Ishihama
(2006).
Characterization of copper-inducible promoters regulated by CpxA/CpxR in Escherichia coli.
|
| |
Biosci Biotechnol Biochem,
70,
1688-1695.
|
|
|
|
|
|
|
M.Solà,
D.L.Drew,
A.G.Blanco,
F.X.Gomis-Rüth,
and
M.Coll
(2006).
The cofactor-induced pre-active conformation in PhoB.
|
| |
Acta Crystallogr D Biol Crystallogr,
62,
1046-1057.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
N.Sewald,
S.D.Wilking,
R.Eckel,
S.Albu,
K.Wollschläger,
K.Gaus,
A.Becker,
F.W.Bartels,
R.Ros,
and
D.Anselmetti
(2006).
Probing DNA-peptide interaction forces at the single-molecule level.
|
| |
J Pept Sci,
12,
836-842.
|
|
|
|
|
|
|
R.J.Fischer,
S.Oehmcke,
U.Meyer,
M.Mix,
K.Schwarz,
T.Fiedler,
and
H.Bahl
(2006).
Transcription of the pst operon of Clostridium acetobutylicum is dependent on phosphate concentration and pH.
|
| |
J Bacteriol,
188,
5469-5478.
|
|
|
|
|
|
|
V.Jensen,
D.Löns,
C.Zaoui,
F.Bredenbruch,
A.Meissner,
G.Dieterich,
R.Münch,
and
S.Häussler
(2006).
RhlR expression in Pseudomonas aeruginosa is modulated by the Pseudomonas quinolone signal via PhoB-dependent and -independent pathways.
|
| |
J Bacteriol,
188,
8601-8606.
|
|
|
|
|
|
|
Z.C.Yuan,
R.Zaheer,
R.Morton,
and
T.M.Finan
(2006).
Genome prediction of PhoB regulated promoters in Sinorhizobium meliloti and twelve proteobacteria.
|
| |
Nucleic Acids Res,
34,
2686-2697.
|
|
|
|
|
|
|
Z.C.Yuan,
R.Zaheer,
and
T.M.Finan
(2006).
Regulation and properties of PstSCAB, a high-affinity, high-velocity phosphate transport system of Sinorhizobium meliloti.
|
| |
J Bacteriol,
188,
1089-1102.
|
|
|
|
|
|
|
A.A.Gusa,
and
J.R.Scott
(2005).
The CovR response regulator of group A streptococcus (GAS) acts directly to repress its own promoter.
|
| |
Mol Microbiol,
56,
1195-1207.
|
|
|
|
|
|
|
A.Sola-Landa,
A.Rodríguez-García,
E.Franco-Domínguez,
and
J.F.Martín
(2005).
Binding of PhoP to promoters of phosphate-regulated genes in Streptomyces coelicolor: identification of PHO boxes.
|
| |
Mol Microbiol,
56,
1373-1385.
|
|
|
|
|
|
|
A.Toro-Roman,
T.Wu,
and
A.M.Stock
(2005).
A common dimerization interface in bacterial response regulators KdpE and TorR.
|
| |
Protein Sci,
14,
3077-3088.
|
|
|
PDB codes:
|
|
|
|
|
|
|
|
F.Depardieu,
P.Courvalin,
and
A.Kolb
(2005).
Binding sites of VanRB and sigma70 RNA polymerase in the vanB vancomycin resistance operon of Enterococcus faecium BM4524.
|
| |
Mol Microbiol,
57,
550-564.
|
|
|
|
|
|
|
J.Gao,
A.A.Gusa,
J.R.Scott,
and
G.Churchward
(2005).
Binding of the global response regulator protein CovR to the sag promoter of Streptococcus pyogenes reveals a new mode of CovR-DNA interaction.
|
| |
J Biol Chem,
280,
38948-38956.
|
|
|
|
|
|
|
K.Welfle,
F.Pratto,
R.Misselwitz,
J.Behlke,
J.C.Alonso,
and
H.Welfle
(2005).
Role of the N-terminal region and of beta-sheet residue Thr29 on the activity of the omega2 global regulator from the broad-host range Streptococcus pyogenes plasmid pSM19035.
|
| |
Biol Chem,
386,
881-894.
|
|
|
|
|
|
|
P.Bachhawat,
G.V.Swapna,
G.T.Montelione,
and
A.M.Stock
(2005).
Mechanism of activation for transcription factor PhoB suggested by different modes of dimerization in the inactive and active states.
|
| |
Structure,
13,
1353-1363.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
R.Eckel,
S.D.Wilking,
A.Becker,
N.Sewald,
R.Ros,
and
D.Anselmetti
(2005).
Single-molecule experiments in synthetic biology: an approach to the affinity ranking of DNA-binding peptides.
|
| |
Angew Chem Int Ed Engl,
44,
3921-3924.
|
|
|
|
|
|
|
W.R.McCleary
(2005).
No phobias about PhoB activation.
|
| |
Structure,
13,
1238-1239.
|
|
|
|
|
|
|
H.Geng,
S.Nakano,
and
M.M.Nakano
(2004).
Transcriptional activation by Bacillus subtilis ResD: tandem binding to target elements and phosphorylation-dependent and -independent transcriptional activation.
|
| |
J Bacteriol,
186,
2028-2037.
|
|
|
|
|
|
|
S.Lejona,
M.E.Castelli,
M.L.Cabeza,
L.J.Kenney,
E.García Véscovi,
and
F.C.Soncini
(2004).
PhoP can activate its target genes in a PhoQ-independent manner.
|
| |
J Bacteriol,
186,
2476-2480.
|
|
|
|
|
|
|
T.L.Dalton,
and
J.R.Scott
(2004).
CovS inactivates CovR and is required for growth under conditions of general stress in Streptococcus pyogenes.
|
| |
J Bacteriol,
186,
3928-3937.
|
|
|
|
|
|
|
Y.Chen,
W.R.Abdel-Fattah,
and
F.M.Hulett
(2004).
Residues required for Bacillus subtilis PhoP DNA binding or RNA polymerase interaction: alanine scanning of PhoP effector domain transactivation loop and alpha helix 3.
|
| |
J Bacteriol,
186,
1493-1502.
|
|
|
|
|
|
|
A.Howell,
S.Dubrac,
K.K.Andersen,
D.Noone,
J.Fert,
T.Msadek,
and
K.Devine
(2003).
Genes controlled by the essential YycG/YycF two-component system of Bacillus subtilis revealed through a novel hybrid regulator approach.
|
| |
Mol Microbiol,
49,
1639-1655.
|
|
|
|
|
|
|
C.Birck,
Y.Chen,
F.M.Hulett,
and
J.P.Samama
(2003).
The crystal structure of the phosphorylation domain in PhoP reveals a functional tandem association mediated by an asymmetric interface.
|
| |
J Bacteriol,
185,
254-261.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
C.Laguri,
M.K.Phillips-Jones,
and
M.P.Williamson
(2003).
Solution structure and DNA binding of the effector domain from the global regulator PrrA (RegA) from Rhodobacter sphaeroides: insights into DNA binding specificity.
|
| |
Nucleic Acids Res,
31,
6778-6787.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
E.S.Krukonis,
and
V.J.DiRita
(2003).
DNA binding and ToxR responsiveness by the wing domain of TcpP, an activator of virulence gene expression in Vibrio cholerae.
|
| |
Mol Cell,
12,
157-165.
|
|
|
|
|
|
|
K.A.Kalivoda,
S.M.Steenbergen,
E.R.Vimr,
and
J.Plumbridge
(2003).
Regulation of sialic acid catabolism by the DNA binding protein NanR in Escherichia coli.
|
| |
J Bacteriol,
185,
4806-4815.
|
|
|
|
|
|
|
R.García-Castellanos,
A.Marrero,
G.Mallorquí-Fernández,
J.Potempa,
M.Coll,
and
F.X.Gomis-Ruth
(2003).
Three-dimensional structure of MecI. Molecular basis for transcriptional regulation of staphylococcal methicillin resistance.
|
| |
J Biol Chem,
278,
39897-39905.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
T.Stein,
S.Heinzmann,
P.Kiesau,
B.Himmel,
and
K.D.Entian
(2003).
The spa-box for transcriptional activation of subtilin biosynthesis and immunity in Bacillus subtilis.
|
| |
Mol Microbiol,
47,
1627-1636.
|
|
|
|
|
|
|
V.L.Robinson,
T.Wu,
and
A.M.Stock
(2003).
Structural analysis of the domain interface in DrrB, a response regulator of the OmpR/PhoB subfamily.
|
| |
J Bacteriol,
185,
4186-4194.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
Y.Chen,
C.Birck,
J.P.Samama,
and
F.M.Hulett
(2003).
Residue R113 is essential for PhoP dimerization and function: a residue buried in the asymmetric PhoP dimer interface determined in the PhoPN three-dimensional crystal structure.
|
| |
J Bacteriol,
185,
262-273.
|
|
|
|
|
|
|
A.E.Maris,
M.R.Sawaya,
M.Kaczor-Grzeskowiak,
M.R.Jarvis,
S.M.Bearson,
M.L.Kopka,
I.Schröder,
R.P.Gunsalus,
and
R.E.Dickerson
(2002).
Dimerization allows DNA target site recognition by the NarL response regulator.
|
| |
Nat Struct Biol,
9,
771-778.
|
|
|
PDB code:
|
|
|
|
|
|
|
|
K.Mattison,
R.Oropeza,
and
L.J.Kenney
(2002).
The linker region plays an important role in the interdomain communication of the response regulator OmpR.
|
| |
J Biol Chem,
277,
32714-32721.
|
|
|
|
|
|
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.
|
|
Links
