Sequential conformational transitions and alpha-helical supercoiling regulate a sensor histidine kinase
Artikel i vetenskaplig tidskrift, 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.
Författare
Oskar Berntsson
Göteborgs universitet
Ralph P. Diensthuber
Humboldt-Universität zu Berlin
Matthijs Panman
Institutionen för kemi, GU
Alexander Björling
Göteborgs universitet
Emil Gustavsson
Göteborgs universitet
Chalmers, Matematiska vetenskaper
Maria Hoernke
Göteborgs universitet
Ashley Hughes
Göteborgs universitet
Léocadie Henry
Göteborgs universitet
Stephan Niebling
Göteborgs universitet
Heikki Takala
Helsingin Yliopisto
Göteborgs universitet
Janne A. Ihalainen
Jyväskylän Yliopisto
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
Department of Chemistry, The University of Chicago
Irina Kosheleva
Department of Chemistry, The University of Chicago
Andreas Möglich
Universität Bayreuth
Humboldt-Universität zu Berlin
Sebastian Westenhoff
Institutionen för kemi, GU
Nature Communications
2041-1723 (ISSN) 20411723 (eISSN)
Vol. 8 1 284Ämneskategorier (SSIF 2025)
Molekylärbiologi
DOI
10.1038/s41467-017-00300-5