Sequential conformational transitions and alpha-helical supercoiling regulate a sensor histidine kinase
Journal article, 2017
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.
Author
Oskar Berntsson
University of Gothenburg
Ralph P. Diensthuber
Humboldt University of Berlin
Matthijs Panman
University of Gothenburg
Alexander Björling
University of Gothenburg
Emil Gustavsson
Chalmers, Mathematical Sciences
University of Gothenburg
Maria Hoernke
University of Gothenburg
Ashley Hughes
University of Gothenburg
Léocadie Henry
University of Gothenburg
Stephan Niebling
University of Gothenburg
Heikki Takala
University of Helsinki
University of Gothenburg
Janne A. Ihalainen
University of Jyväskylä
Gemma Newby
European Synchrotron Radiation Facility (ESRF)
Silke Kerruth
Freie Universität Berlin
Joachim Heberle
Freie Universität Berlin
Marianne Liebi
Paul Scherrer Institut
Andreas Menzel
Paul Scherrer Institut
Robert Henning
University of Chicago
Irina Kosheleva
University of Chicago
Andreas Möglich
Humboldt University of Berlin
University of Bayreuth
Sebastian Westenhoff
University of Gothenburg
Nature Communications
2041-1723 (ISSN) 20411723 (eISSN)
Vol. 8 1 284Subject Categories (SSIF 2025)
Molecular Biology
DOI
10.1038/s41467-017-00300-5