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Nat Commun. 2017 Aug 18;8(1):284. doi: 10.1038/s41467-017-00300-5.

Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase.

Author information

1
University of Gothenburg, 40530, Gothenburg, Sweden.
2
Humboldt-Universität zu Berlin, Berlin, 10115, Germany.
3
Albert-Ludwigs-Universität Freiburg, 79104, Freiburg i.Br., Germany.
4
University of Jyväskylä, 40014, Jyväskylä, Finland.
5
University of Helsinki, 00014, Helsinki, Finland.
6
European Synchrotron Radiation Facility, 38000, Grenoble, France.
7
Freie Universität Berlin, 14195, Berlin, Germany.
8
Paul ScherrerInstitut, 5232, Villigen, Switzerland.
9
The University of Chicago, Chicago, IL, 60637, USA.
10
Humboldt-Universität zu Berlin, Berlin, 10115, Germany. andreas.moeglich@uni-bayreuth.de.
11
Universität Bayreuth, Bayreuth, 95440, Germany. andreas.moeglich@uni-bayreuth.de.
12
University of Gothenburg, 40530, Gothenburg, Sweden. westenho@chem.gu.se.

Abstract

Sensor histidine kinases are central to sensing in bacteria and in plants. They usually contain sensor, linker, and kinase modules and the structure of many of these components is known. However, it is unclear how the kinase module is structurally regulated. Here, we use nano- to millisecond time-resolved X-ray scattering to visualize the solution structural changes that occur when the light-sensitive model histidine kinase YF1 is activated by blue light. We find that the coiled coil linker and the attached histidine kinase domains undergo a left handed rotation within microseconds. In a much slower second step, the kinase domains rearrange internally. This structural mechanism presents a template for signal transduction in sensor histidine kinases.Sensor histidine kinases (SHK) consist of sensor, linker and kinase modules and different models for SHK signal transduction have been proposed. Here the authors present nano- to millisecond time-resolved X-ray scattering measurements, which reveal a structural mechanism for kinase domain activation in SHK.

PMID:
28819239
PMCID:
PMC5561222
DOI:
10.1038/s41467-017-00300-5
[Indexed for MEDLINE]
Free PMC Article

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