Nature Communications (Aug 2017)
Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
- Oskar Berntsson,
- Ralph P. Diensthuber,
- Matthijs R. Panman,
- Alexander Björling,
- Emil Gustavsson,
- Maria Hoernke,
- Ashley J. Hughes,
- Léocadie Henry,
- Stephan Niebling,
- Heikki Takala,
- Janne A. Ihalainen,
- Gemma Newby,
- Silke Kerruth,
- Joachim Heberle,
- Marianne Liebi,
- Andreas Menzel,
- Robert Henning,
- Irina Kosheleva,
- Andreas Möglich,
- Sebastian Westenhoff
Affiliations
- Oskar Berntsson
- University of Gothenburg
- Ralph P. Diensthuber
- Humboldt-Universität zu Berlin
- Matthijs R. Panman
- University of Gothenburg
- Alexander Björling
- University of Gothenburg
- Emil Gustavsson
- University of Gothenburg
- Maria Hoernke
- University of Gothenburg
- Ashley J. Hughes
- University of Gothenburg
- Léocadie Henry
- University of Gothenburg
- Stephan Niebling
- University of Gothenburg
- Heikki Takala
- University of Gothenburg
- Janne A. Ihalainen
- University of Jyväskylä
- Gemma Newby
- European Synchrotron Radiation Facility
- Silke Kerruth
- Freie Universität Berlin
- Joachim Heberle
- Freie Universität Berlin
- Marianne Liebi
- Paul ScherrerInstitut
- Andreas Menzel
- Paul ScherrerInstitut
- Robert Henning
- The University of Chicago
- Irina Kosheleva
- The University of Chicago
- Andreas Möglich
- Humboldt-Universität zu Berlin
- Sebastian Westenhoff
- University of Gothenburg
- DOI
- https://doi.org/10.1038/s41467-017-00300-5
- Journal volume & issue
-
Vol. 8,
no. 1
pp. 1 – 8
Abstract
Sensor histidine kinases (SHK) consist of sensor, linker and kinase modules and different models for SHK signal transduction have been proposed. Here the authors present nano- to millisecond time-resolved X-ray scattering measurements, which reveal a structural mechanism for kinase domain activation in SHK.
