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* Residue conservation analysis
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DOI no:
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Structure
11:1097-1110
(2003)
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PubMed id:
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Structure of the oxygen sensor in Bacillus subtilis: signal transduction of chemotaxis by control of symmetry.
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W.Zhang,
G.N.Phillips.
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ABSTRACT
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Much is now known about chemotaxis signaling transduction for Escherichia coli
and Salmonella typhimurium. The mechanism of chemotaxis of Bacillus subtilis is,
in a sense, reversed. Attractant binding strengthens the activity of histidine
kinase in B. subtilis, instead of an inhibition reaction. The HemAT from B.
subtilis can detect oxygen and transmit the signal to regulatory proteins that
control the direction of flagella rotation. We have determined the crystal
structures of the HemAT sensor domain in liganded and unliganded forms at 2.15 A
and 2.7 A resolution, respectively. The liganded structure reveals a highly
symmetrical organization. Tyrosine70 shows distinct conformational changes on
one subunit when ligands are removed. Our study suggests that disruption of the
symmetry of HemAT plays an important role in initiating the chemotaxis signaling
transduction cascade.
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Selected figure(s)
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Figure 1.
Figure 1. The Molecular Structure of the HemAT Sensor
Domain Represented with Ribbon Diagrams(A) Stereo view of the
structure. The signaling domain would be located further down on
the page.(B) Top view showing the flanking of the core helices,
G and H, by the rest of the molecule. The helices are labeled
corresponding to the nomenclature of the globin fold. Subunit A,
cyan; subunit B, yellow.
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The above figure is
reprinted
by permission from Cell Press:
Structure
(2003,
11,
1097-1110)
copyright 2003.
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Figure was
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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E.Geuens,
D.Hoogewijs,
M.Nardini,
E.Vinck,
A.Pesce,
L.Kiger,
A.Fago,
L.Tilleman,
S.De Henau,
M.C.Marden,
R.E.Weber,
S.Van Doorslaer,
J.Vanfleteren,
L.Moens,
M.Bolognesi,
and
S.Dewilde
(2010).
Globin-like proteins in Caenorhabditis elegans: in vivo localization, ligand binding and structural properties.
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BMC Biochem,
11,
17.
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PDB codes:
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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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M.Nardini,
A.Pesce,
L.Thijs,
J.A.Saito,
S.Dewilde,
M.Alam,
P.Ascenzi,
M.Coletta,
C.Ciaccio,
L.Moens,
and
M.Bolognesi
(2008).
Archaeal protoglobin structure indicates new ligand diffusion paths and modulation of haem-reactivity.
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EMBO Rep,
9,
157-163.
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PDB codes:
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S.Aono
(2008).
Metal-containing sensor proteins sensing diatomic gas molecules.
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Dalton Trans,
(),
3137-3146.
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S.F.El-Mashtoly,
Y.Gu,
H.Yoshimura,
S.Yoshioka,
S.Aono,
and
T.Kitagawa
(2008).
Protein conformation changes of HemAT-Bs upon ligand binding probed by ultraviolet resonance Raman spectroscopy.
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J Biol Chem,
283,
6942-6949.
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H.Szurmant,
R.A.White,
and
J.A.Hoch
(2007).
Sensor complexes regulating two-component signal transduction.
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Curr Opin Struct Biol,
17,
706-715.
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K.Wuichet,
R.P.Alexander,
and
I.B.Zhulin
(2007).
Comparative genomic and protein sequence analyses of a complex system controlling bacterial chemotaxis.
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Methods Enzymol,
422,
1.
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L.Thijs,
E.Vinck,
A.Bolli,
F.Trandafir,
X.Wan,
D.Hoogewijs,
M.Coletta,
A.Fago,
R.E.Weber,
S.Van Doorslaer,
P.Ascenzi,
M.Alam,
L.Moens,
and
S.Dewilde
(2007).
Characterization of a globin-coupled oxygen sensor with a gene-regulating function.
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J Biol Chem,
282,
37325-37340.
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M.Makino,
H.Sugimoto,
H.Sawai,
N.Kawada,
K.Yoshizato,
and
Y.Shiro
(2006).
High-resolution structure of human cytoglobin: identification of extra N- and C-termini and a new dimerization mode.
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Acta Crystallogr D Biol Crystallogr,
62,
671-677.
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PDB code:
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S.N.Vinogradov,
D.Hoogewijs,
X.Bailly,
R.Arredondo-Peter,
J.Gough,
S.Dewilde,
L.Moens,
and
J.R.Vanfleteren
(2006).
A phylogenomic profile of globins.
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BMC Evol Biol,
6,
31.
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E.A.Sickmier,
D.Brekasis,
S.Paranawithana,
J.B.Bonanno,
M.S.Paget,
S.K.Burley,
and
C.L.Kielkopf
(2005).
X-ray structure of a Rex-family repressor/NADH complex insights into the mechanism of redox sensing.
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Structure,
13,
43-54.
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PDB code:
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J.J.Miranda,
D.H.Maillett,
J.Soman,
and
J.S.Olson
(2005).
Thermoglobin, oxygen-avid hemoglobin in a bacterial hyperthermophile.
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J Biol Chem,
280,
36754-36761.
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J.W.Murray,
O.Delumeau,
and
R.J.Lewis
(2005).
Structure of a nonheme globin in environmental stress signaling.
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Proc Natl Acad Sci U S A,
102,
17320-17325.
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PDB code:
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W.Zhang,
J.S.Olson,
and
G.N.Phillips
(2005).
Biophysical and kinetic characterization of HemAT, an aerotaxis receptor from Bacillus subtilis.
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Biophys J,
88,
2801-2814.
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H.Szurmant,
and
G.W.Ordal
(2004).
Diversity in chemotaxis mechanisms among the bacteria and archaea.
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Microbiol Mol Biol Rev,
68,
301-319.
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J.Green,
and
M.S.Paget
(2004).
Bacterial redox sensors.
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Nat Rev Microbiol,
2,
954-966.
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T.A.Freitas,
S.Hou,
E.M.Dioum,
J.A.Saito,
J.Newhouse,
G.Gonzalez,
M.A.Gilles-Gonzalez,
and
M.Alam
(2004).
Ancestral hemoglobins in Archaea.
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Proc Natl Acad Sci U S A,
101,
6675-6680.
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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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