8UPM
Pfr state of Stigmatella aurantiaca bacteriophytochrome 2
Summary for 8UPM
Entry DOI | 10.2210/pdb8upm/pdb |
EMDB information | 42452 |
Descriptor | Bacteriophytochrome (Light-regulated signal transduction histidine kinase), BILIVERDINE IX ALPHA (2 entities in total) |
Functional Keywords | red light photoreceptor, two component system, signaling protein |
Biological source | Stigmatella aurantiaca |
Total number of polymer chains | 2 |
Total formula weight | 163466.81 |
Authors | Malla, T.N.,Schmidt, M.,Stojkovic, E.A. (deposition date: 2023-10-23, release date: 2024-09-25, Last modification date: 2024-11-06) |
Primary citation | Malla, T.N.,Hernandez, C.,Muniyappan, S.,Menendez, D.,Bizhga, D.,Mendez, J.H.,Schwander, P.,Stojkovic, E.A.,Schmidt, M. Photoreception and signaling in bacterial phytochrome revealed by single-particle cryo-EM. Sci Adv, 10:eadq0653-eadq0653, 2024 Cited by PubMed Abstract: Phytochromes are red-light photoreceptors discovered in plants with homologs in bacteria and fungi that regulate a variety of physiological responses. They display a reversible photocycle between two distinct states: a red-light-absorbing Pr state and a far-red light-absorbing Pfr state. The photoconversion regulates the activity of an enzymatic domain, usually a histidine kinase (HK). The molecular mechanism that explains how light controls the HK activity is not understood because structures of unmodified bacterial phytochromes with HK activity are missing. Here, we report three cryo-electron microscopy structures of a wild-type bacterial phytochrome with HK activity determined as Pr and Pfr homodimers and as a Pr/Pfr heterodimer with individual subunits in distinct states. We propose that the Pr/Pfr heterodimer is a physiologically relevant signal transduction intermediate. Our results offer insight into the molecular mechanism that controls the enzymatic activity of the HK as part of a bacterial two-component system that perceives and transduces light signals. PubMed: 39121216DOI: 10.1126/sciadv.adq0653 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.75 Å) |
Structure validation
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