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

Berntsson, O; Diensthuber, RP; Panman, MR; Björling, A; Gustavsson, E; Hoernke, M; Hughes, AJ; Henry, L; Niebling, S; Takala, H; et al. Berntsson, O; Diensthuber, RP; Panman, MR; Björling, A; Gustavsson, E; Hoernke, M; Hughes, AJ; Henry, L; Niebling, S; Takala, H; Ihalainen, JA; Newby, G; Kerruth, S; Heberle, J; Liebi, M; Menzel, A; Henning, R; Kosheleva, I; Möglich, A; Westenhoff, S (2017) Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase. Nat Commun, 8 (1). p. 284. ISSN 2041-1723 https://doi.org/10.1038/s41467-017-00300-5
SGUL Authors: Kerruth, Silke

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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
Additional Information: Open Access This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit http://creativecommons.org/licenses/by/4.0/. © The Author(s) 2017
Keywords: MD Multidisciplinary
SGUL Research Institute / Research Centre: Academic Structure > Molecular and Clinical Sciences Research Institute (MCS)
Journal or Publication Title: Nat Commun
ISSN: 2041-1723
Language: eng
Dates:
DateEvent
18 August 2017Published
20 June 2017Accepted
Publisher License: Creative Commons: Attribution 4.0
PubMed ID: 28819239
Go to PubMed abstract
URI: https://openaccess.sgul.ac.uk/id/eprint/109099
Publisher's version: https://doi.org/10.1038/s41467-017-00300-5

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