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Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase

Title data

Berntsson, Oskar ; Diensthuber, Ralph P. ; Panman, Matthijs R. ; Björling, Alexander ; Gustavsson, Emil ; Hoernke, Maria ; Hughes, Ashley J. ; Henry, Léocadie ; Niebling, Stephan ; Takala, Heikki ; Ihalainen, Janne A. ; Newby, Gemma ; Kerruth, Silke ; Heberle, Joachim ; Liebi, Marianne ; Menzel, Andreas ; Henning, Robert ; Kosheleva, Irina ; Möglich, Andreas ; Westenhoff, Sebastian:
Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase.
In: Nature Communications. Vol. 8 (2017) . - No. 284.
ISSN 2041-1723
DOI: https://doi.org/10.1038/s41467-017-00300-5

Official URL: Volltext

Abstract in another language

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. 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.

Further data

Item Type: Article in a journal
Refereed: Yes
Institutions of the University: Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry > Chair Biochemistry - Univ.-Prof. Dr. Andreas Möglich
Faculties
Faculties > Faculty of Biology, Chemistry and Earth Sciences
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry
Faculties > Faculty of Biology, Chemistry and Earth Sciences > Department of Chemistry > Chair Biochemistry
Result of work at the UBT: Yes
DDC Subjects: 500 Science > 570 Life sciences, biology
Date Deposited: 21 Aug 2017 06:14
Last Modified: 21 Aug 2017 06:14
URI: https://eref.uni-bayreuth.de/id/eprint/39142