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PDBsum entry 3g6b
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Signaling protein
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PDB id
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3g6b
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Contents |
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* Residue conservation analysis
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Biochemistry
48:1936-1944
(2009)
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PubMed id:
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The structure of a soluble chemoreceptor suggests a mechanism for propagating conformational signals.
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A.M.Pollard,
A.M.Bilwes,
B.R.Crane.
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ABSTRACT
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Transmembrane chemoreceptors, also known as methyl-accepting chemotaxis proteins
(MCPs), translate extracellular signals into intracellular responses in the
bacterial chemotaxis system. MCP ligand binding domains control the activity of
the CheA kinase, situated approximately 200 A away, across the cytoplasmic
membrane. The 2.17 A resolution crystal structure of a Thermotoga maritima
soluble receptor (Tm14) reveals distortions in its dimeric four-helix bundle
that provide insight into the conformational states available to MCPs for
propagating signals. A bulge in one helix generates asymmetry between subunits
that displaces the kinase-interacting tip, which resides more than 100 A away.
The maximum bundle distortion maps to the adaptation region of transmembrane
MCPs where reversible methylation of acidic residues tunes receptor activity.
Minor alterations in coiled-coil packing geometry translate the bulge distortion
to a >25 A movement of the tip relative to the bundle stalks. The Tm14
structure discloses how alterations in local helical structure, which could be
induced by changes in methylation state and/or by conformational signals from
membrane proximal regions, can reposition a remote domain that interacts with
the CheA kinase.
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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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T.Krell,
J.Lacal,
F.Muñoz-Martínez,
J.A.Reyes-Darias,
B.H.Cadirci,
C.García-Fontana,
and
J.L.Ramos
(2011).
Diversity at its best: bacterial taxis.
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Environ Microbiol,
13,
1115-1124.
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D.J.Fowler,
R.M.Weis,
and
L.K.Thompson
(2010).
Kinase-active signaling complexes of bacterial chemoreceptors do not contain proposed receptor-receptor contacts observed in crystal structures.
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Biochemistry,
49,
1425-1434.
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D.N.Amin,
and
G.L.Hazelbauer
(2010).
Chemoreceptors in signalling complexes: shifted conformation and asymmetric coupling.
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Mol Microbiol,
78,
1313-1323.
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J.Bhatnagar,
P.P.Borbat,
A.M.Pollard,
A.M.Bilwes,
J.H.Freed,
and
B.R.Crane
(2010).
Structure of the ternary complex formed by a chemotaxis receptor signaling domain, the CheA histidine kinase, and the coupling protein CheW as determined by pulsed dipolar ESR spectroscopy.
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Biochemistry,
49,
3824-3841.
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J.Lacal,
C.García-Fontana,
F.Muñoz-Martínez,
J.L.Ramos,
and
T.Krell
(2010).
Sensing of environmental signals: classification of chemoreceptors according to the size of their ligand binding regions.
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Environ Microbiol,
12,
2873-2884.
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B.E.Scharf,
P.D.Aldridge,
J.R.Kirby,
and
B.R.Crane
(2009).
Upward mobility and alternative lifestyles: a report from the 10th biennial meeting on Bacterial Locomotion and Signal Transduction.
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Mol Microbiol,
73,
5.
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D.Albanesi,
M.Martín,
F.Trajtenberg,
M.C.Mansilla,
A.Haouz,
P.M.Alzari,
D.de Mendoza,
and
A.Buschiazzo
(2009).
Structural plasticity and catalysis regulation of a thermosensor histidine kinase.
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Proc Natl Acad Sci U S A,
106,
16185-16190.
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PDB codes:
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K.E.Swain,
M.A.Gonzalez,
and
J.J.Falke
(2009).
Engineered socket study of signaling through a four-helix bundle: evidence for a yin-yang mechanism in the kinase control module of the aspartate receptor.
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Biochemistry,
48,
9266-9277.
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Q.Zhou,
P.Ames,
and
J.S.Parkinson
(2009).
Mutational analyses of HAMP helices suggest a dynamic bundle model of input-output signalling in chemoreceptors.
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Mol Microbiol,
73,
801-814.
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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
