Sequential conformational transitions and alpha-helical supercoiling regulate a sensor histidine kinase
| Autor: | Berntsson, Oskar, Diensthuber, Ralph P., Panman, Matthijs R., Björling, Alexander, Gustavsson, Emil, Hoernke, Maria, Hughes, Ashley J., Henry, Leocadie, 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 |
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| Přispěvatelé: | Univ Gothenburg, S-40530 Gothenburg, Sweden, Humboldt State University (HSU), University of Freiburg [Freiburg], University of Jyväskylä (JYU), Univ Helsinki, FIN-00014 Helsinki, Finland, European Synchrotron Radiation Facility (ESRF), Free University of Berlin (FU), Paul Scherrer Inst, CH-5232 Villigen, Switzerland, University of Chicago, Universität Bayreuth, Medicum, University of Helsinki |
| Jazyk: | angličtina |
| Rok vydání: | 2017 |
| Předmět: |
LOV DOMAIN
Models Molecular SIGNALING MECHANISM Histidine Kinase Light PROTEINS Protein Conformation [SDV]Life Sciences [q-bio] STRUCTURAL DYNAMICS Crystallography X-Ray RAY SOLUTION SCATTERING Protein Structure Secondary PHOTOTROPIN BLUE-LIGHT PHOTORECEPTOR Bacterial Proteins Protein Domains X-Ray Diffraction Scattering Small Angle MD Multidisciplinary Nanotechnology TIME-RESOLVED WAXS Science & Technology SMALL-ANGLE SCATTERING Multidisciplinary Sciences Science & Technology - Other Topics 3111 Biomedicine FULL-LENGTH STRUCTURE |
| Zdroj: | Nature Communications Nature Communications, Nature Publishing Group, 2017, 8, 8 p. ⟨10.1038/s41467-017-00300-5⟩ |
| ISSN: | 2041-1723 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
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