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


Ontology type: schema:ScholarlyArticle      Open Access: True


Article Info

DATE

2017-08-18

AUTHORS

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

ABSTRACT

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. More... »

PAGES

284

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/s41467-017-00300-5

DOI

http://dx.doi.org/10.1038/s41467-017-00300-5

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1091148238

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/28819239


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