9MD9 | pdb_00009md9

Observation of early events in the photoactivation of Myxobacterial phytochrome using time-resolved serial femtosecond crystallography.

Malla, T.N., Aldama, L., Leon, V., Feliz, D., Hu, H., Thomas, I., Cellini, A., Wahlgren, W.Y., Nimmrich, A., Botha, S., Sierra, R., Hunter, M.S., Poitevin, F., Lisova, S., Batyuk, A., Gate, G., Jernigan, R., Kupitz, C.J., Maj, P., Meszaros, P., Kurttila, M., Monrroy, L., Luo, F., Owada, S., Kang, J., Slavov, C., Maj, M., Gautier, C., Kashipathy, M., Tolstikova, A., Mariani, V., Barty, A., Moss, F., Schwander, P., Liu, H., Boutet, S., Fromme, P., Takala, H., Ihalainen, J.A., Weierstall, U., Westenhoff, S., Stojkovic, E.A., Schmidt, M.

(2025) Commun Chem 8: 183-183

• PubMed: 40506475 Search on PubMedSearch on PubMed Central
• DOI: https://doi.org/10.1038/s42004-025-01578-z
• Primary Citation of Related Structures:  
  9DZ3, 9DZA, 9DZP, 9MD9, 9MEB


• PubMed Abstract: 
  

  Myxobacteria are non-photosynthetic, soil-dwelling bacteria distinguished by a multicellular stage in their life cycle known as fruiting bodies that are stimulated by light. Myxobacterial phytochromes are candidates for the perception of red-light. The mechanism how light is perceived and converted to a physiological response is unknown. Here, time-resolved serial femtosecond crystallographic (TR-SFX) experiments were conducted on microcrystals of the photosensory core module of the Stigmatella aurantiaca bacteriophytochrome 2 (SaBphP2). Initial events of the Z to E isomerization reaction of the covalently bound, open-chain tetrapyrrole biliverdin (BV) chromophore were determined. At 3 ps after light activation, the BV ring-D assumes a configuration needed for the isomerization. At 100 ps, a mixture of BV in the Z or E configuration is observed in subunit A, while in the other subunit the chromophore remains in the Z configuration. In conjunction with prior results, these structures reveal the molecular mechanism of phytochrome activation in the photomorphogenesis of the myxobacteria and provide the molecular foundation for physiological responses to red light in other bacteria.

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Organizational Affiliation: 
• Department of Physics, University of Wisconsin-Milwaukee, Milwaukee, WI, USA.
Vaccine Research Center Electron Microscopy Unit, Frederick National Laboratory for Cancer Research, Frederick, MD, 21702, USA.
Department of Biology, Northeastern Illinois University, Chicago, IL, USA.
Department of Physics, Arizona State University, Tempe, AZ, USA.
Department of Chemistry and Molecular Biology, University of Gothenburg, Gothenburg, Sweden.
Department of Chemistry, University of Washington, Seattle, WA, USA.
Linac Coherent Light Source, SLAC National Accelerator Laboratory, Menlo Park, CA, USA.
School of Molecular Sciences and Biodesign Center for Applied Structural Discovery, Arizona State University, Tempe, USA.
Department of Chemistry-BMC, Uppsala University, Uppsala, Sweden.
Nanoscience Center, Department of Biological and Environmental Science, University of Jyväskylä, Jyväskylä, Finland.
Japan Synchrotron Radiation Research Institute, Hyogo, Japan.
RIKEN SPring-8 Center, Hyogo, Japan.
Department of Chemistry, University of South Florida, Tampa, FL, USA.
Department of Chemistry- Ångström, Uppsala University, Uppsala, Sweden.
Center for Free-Electron Laser Science, Deutsches Elektronen Synchrotron, Hamburg, Germany.
Microsoft Research AI4Science, Beijing, China.
Department of Physics, University of Wisconsin-Milwaukee, Milwaukee, WI, USA. smarius@uwm.edu.
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