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

Institution of Chemistry at Gothenburg University

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 Gothenburg

University of Helsinki

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

Department of Chemistry, The University of Chicago

Irina Kosheleva

Department of Chemistry, The University of Chicago

Andreas Möglich

University of Bayreuth

Humboldt University of Berlin

Sebastian Westenhoff

Institution of Chemistry at Gothenburg University

Nature Communications

2041-1723 (ISSN) 20411723 (eISSN)

Vol. 8 1 284

Subject Categories (SSIF 2025)

Molecular Biology

DOI

10.1038/s41467-017-00300-5

More information

Latest update

7/1/2025 8