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


Berntsson, Oskar, Diensthuber, Ralph P, Panman, Matthijs R, Bjorling, Alexander, Gustavsson, Emil, Hoernke, Maria, Hughes, Ashley J ORCID: 0000-0001-5432-5271, Henry, Leocadie, Niebling, Stephan, Takala, Heikki et al (show 10 more authors) (2017) Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase. NATURE COMMUNICATIONS, 8 (1). 284-.

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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.

Item Type: Article
Uncontrolled Keywords: Bacterial Proteins, X-Ray Diffraction, Crystallography, X-Ray, Protein Conformation, Protein Structure, Secondary, Nanotechnology, Light, Models, Molecular, Scattering, Small Angle, Histidine Kinase, Protein Domains
Depositing User: Symplectic Admin
Date Deposited: 27 Feb 2019 11:12
Last Modified: 09 Oct 2023 21:59
DOI: 10.1038/s41467-017-00300-5
Open Access URL: https://doi.org/10.1038/s41467-017-00300-5
Related URLs:
URI: https://livrepository.liverpool.ac.uk/id/eprint/3033502
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