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4GCZ

Structure of a blue-light photoreceptor

Summary for 4GCZ
Entry DOI10.2210/pdb4gcz/pdb
Related2PR5
DescriptorBlue-light photoreceptor, Sensor protein fixL, FLAVIN MONONUCLEOTIDE, ADENOSINE-5'-DIPHOSPHATE, ... (5 entities in total)
Functional Keywordsphotoreceptor, signal transduction, two-component system, light-oxygen-voltage, per-arnt-sim, dhp, sensor histidine kinase, signaling protein, de novo protein
Biological sourceBacillus subtilis
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Total number of polymer chains2
Total formula weight88775.90
Authors
Diensthuber, R.P.,Bommer, M.,Moglich, A. (deposition date: 2012-07-31, release date: 2013-06-19, Last modification date: 2024-10-16)
Primary citationDiensthuber, R.P.,Bommer, M.,Gleichmann, T.,Moglich, A.
Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators.
Structure, 21:1127-1136, 2013
Cited by
PubMed Abstract: 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.
PubMed: 23746806
DOI: 10.1016/j.str.2013.04.024
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.3 Å)
Structure validation

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