Sequential conformational transitions and α-helical supercoiling regulate a sensor histidine kinase
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
Published inNature Communications
© the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.
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.
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Except where otherwise noted, this item's license is described as © the Authors, 2017. This article is licensed under a Creative Commons Attribution 4.0 International License.
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