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

Chalmers, Matematiska vetenskaper

Göteborgs universitet

Maria Hoernke

Göteborgs universitet

Ashley Hughes

Göteborgs universitet

Léocadie Henry

Göteborgs universitet

Stephan Niebling

Göteborgs universitet

Heikki Takala

Göteborgs universitet

Helsingin Yliopisto

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 1 284

Ämneskategorier (SSIF 2025)

Molekylärbiologi

DOI

10.1038/s41467-017-00300-5

Mer information

Senast uppdaterat

2025-07-01