Molecular asymmetry of a photosynthetic supercomplex from green sulfur bacteria.

Autor: Puskar R; School of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA., Du Truong C; School of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.; Rampart Bioscience, Monrovia, CA, 91016, USA., Swain K; School for Engineering of Matter, Transport and Energy, Arizona State University, Tempe, AZ, 85287, USA., Chowdhury S; School of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA., Chan KY; School of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA., Li S; Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA., Cheng KW; Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA., Wang TY; Proteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA, 91125, USA., Poh YP; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.; Center for Mechanisms of Evolution, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA., Mazor Y; School of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA.; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA., Liu H; Department of Biology, Washington University, St. Louis, MO, 63130, USA., Chou TF; Division of Biology and Biological Engineering, California Institute of Technology, Pasadena, CA, 91125, USA.; Proteome Exploration Laboratory, Beckman Institute, California Institute of Technology, Pasadena, CA, 91125, USA., Nannenga BL; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA.; School for Engineering of Matter, Transport and Energy, Arizona State University, Tempe, AZ, 85287, USA., Chiu PL; School of Molecular Sciences, Arizona State University, Tempe, AZ, 85287, USA. plchiu@asu.edu.; Center for Applied Structural Discovery, Biodesign Institute, Arizona State University, Tempe, AZ, 85287, USA. plchiu@asu.edu.
Jazyk: angličtina
Zdroj: Nature communications [Nat Commun] 2022 Oct 03; Vol. 13 (1), pp. 5824. Date of Electronic Publication: 2022 Oct 03.
DOI: 10.1038/s41467-022-33505-4
Abstrakt: The photochemical reaction center (RC) features a dimeric architecture for charge separation across the membrane. In green sulfur bacteria (GSB), the trimeric Fenna-Matthews-Olson (FMO) complex mediates the transfer of light energy from the chlorosome antenna complex to the RC. Here we determine the structure of the photosynthetic supercomplex from the GSB Chlorobaculum tepidum using single-particle cryogenic electron microscopy (cryo-EM) and identify the cytochrome c subunit (PscC), two accessory protein subunits (PscE and PscF), a second FMO trimeric complex, and a linker pigment between FMO and the RC core. The protein subunits that are assembled with the symmetric RC core generate an asymmetric photosynthetic supercomplex. One linker bacteriochlorophyll (BChl) is located in one of the two FMO-PscA interfaces, leading to differential efficiencies of the two energy transfer branches. The two FMO trimeric complexes establish two different binding interfaces with the RC cytoplasmic surface, driven by the associated accessory subunits. This structure of the GSB photosynthetic supercomplex provides mechanistic insight into the light excitation energy transfer routes and a possible evolutionary transition intermediate of the bacterial photosynthetic supercomplex from the primitive homodimeric RC.
(© 2022. The Author(s).)
Databáze: MEDLINE
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