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

Journal article
Authors Oskar Berntsson
R. P. Diensthuber
Matthijs R Panman
Alexander Björling
Emil Gustavsson
Maria Hoernke
Ashley J Hughes
Léocadie Henry
Stephan Niebling
Heikki Takala
J. A. Ihalainen
G. Newby
S. Kerruth
J. Heberle
M. Liebi
A. Menzel
R. Henning
I. Kosheleva
A. Moglich
Sebastian Westenhoff
Published in Nature Communications
Volume 8
ISSN 2041-1723
Publication year 2017
Published at Department of Mathematical Sciences
Department of Chemistry and Molecular Biology
Language en
Keywords blue-light photoreceptor, ray solution scattering, small-angle, scattering, full-length structure, time-resolved waxs, structural, dynamics, signaling mechanism, lov domain, phototropin, proteins, Science & Technology - Other Topics
Subject categories Biological Sciences, Chemical Sciences


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.

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