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Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators

Title data

Diensthuber, Ralph P. ; Bommer, Martin ; Gleichmann, Tobias ; Möglich, Andreas:
Full-length structure of a sensor histidine kinase pinpoints coaxial coiled coils as signal transducers and modulators.
In: Structure. Vol. 21 (2 July 2013) Issue 7 . - pp. 1127-1136.
ISSN 0969-2126
DOI: https://doi.org/10.1016/j.str.2013.04.024

Project information

Project financing: Alexander von Humboldt-Stiftung

Abstract in another language

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.

Further data

Item Type: Article in a journal
Refereed: Yes
Additional notes: PubMed-ID: 23746806
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Professorship Biochemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: No
DDC Subjects: 500 Science > 540 Chemistry
Date Deposited: 19 May 2015 07:30
Last Modified: 19 May 2015 07:30
URI: https://eref.uni-bayreuth.de/id/eprint/13597