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PDBsum entry 4gcz
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Signaling protein, de novo protein
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PDB id
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4gcz
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References listed in PDB file
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Key reference
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Title
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Full-Length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators.
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Authors
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R.P.Diensthuber,
M.Bommer,
T.Gleichmann,
A.Möglich.
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Ref.
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Structure, 2013,
21,
1127-1136.
[DOI no: ]
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PubMed id
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Abstract
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Two-component systems (TCSs), which comprise sensor histidine kinases (SHK) and
response-regulator proteins, represent the predominant strategy by which
prokaryotes sense and respond to a changing environment. Despite paramount
biological importance, a dearth exists of intact SHK structures containing both
sensor and effector modules. Here, we report the full-length crystal structure
of the engineered, dimeric, blue-light-regulated SHK YF1 at 2.3 Å resolution,
in which two N-terminal light-oxygen-voltage (LOV) photosensors are connected by
a coiled coil to the C-terminal effector modules. A second coaxial coiled coil
derived from the N-termini of the LOV photosensors and inserted between them
crucially modulates light regulation: single mutations within this coiled coil
attenuate or even invert the signal response of the TCS. Structural motifs
identified in YF1 recur in signal receptors, and the underlying signaling
principles and mechanisms may be widely shared between soluble and
transmembrane, prokaryotic, and eukaryotic signal receptors of diverse
biological activity.
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