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

• Published in: Nature communications Vol. 8; no. 1; pp. 284 - 8
• Main Authors: 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
• Format: Journal Article
• Language: English
• Published: London Nature Publishing Group UK 18.08.2017; Nature Publishing Group; Nature Portfolio
• Subjects: 631/45/275; 631/535; 631/57; 631/57/2266; Bacterial Proteins - chemistry; Bacterial Proteins - metabolism; Biological Sciences; Biologiska vetenskaper; blue-light photoreceptor; Chemical Sciences; Crystallography, X-Ray; dynamics; full-length structure; Histidine; Histidine kinase; Histidine Kinase - chemistry; Histidine Kinase - metabolism; Humanities and Social Sciences; Kemi; Kinases; Life Sciences; Light; lov domain; Models, Molecular; Modules; multidisciplinary; Nanotechnology; phototropin; Protein Conformation; Protein Domains - radiation effects; Protein Structure, Secondary; proteins; ray solution scattering; Scattering; Scattering, Small Angle; Science; Science & Technology - Other Topics; Science (multidisciplinary); Sensors; Signal transduction; signaling mechanism; small-angle; structural; Supercoiling; time-resolved waxs; X-Ray Diffraction; X-ray scattering
• ISSN: 2041-1723; 2041-1723
• DOI: 10.1038/s41467-017-00300-5

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.