Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
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.
Main Authors
Format
Articles
Research article
Published
2017
Series
Subjects
Publication in research information system
Publisher
Nature Publishing Group
The permanent address of the publication
https://urn.fi/URN:NBN:fi:jyu-201708243558Use this for linking
Review status
Peer reviewed
ISSN
2041-1723
DOI
https://doi.org/10.1038/s41467-017-00300-5
Language
English
Published in
Nature Communications
Citation
- Berntsson, O., Diensthuber, R. P., Panman, M. R., Björling, A., Gustavsson, E., Hoernke, M., Hughes, A. J., Henry, L., Niebling, S., Takala, H., Ihalainen, J., Newby, G., Kerruth, S., Heberle, J., Liebi, M., Menzel, A., Henning, R., Kosheleva, I., Möglich, A., & Westenhoff, S. (2017). Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase. Nature Communications, 8, Article 284. https://doi.org/10.1038/s41467-017-00300-5
License
Copyright© the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.