Molecular asymmetry of a photosynthetic supercomplex from green sulfur bacteria
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| Titel: | Molecular asymmetry of a photosynthetic supercomplex from green sulfur bacteria |
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| Autoren: | Puskar, Ryan, Du Truong, Chloe, Swain, Kyle, Chowdhury, Saborni, Chan, Ka-Yi, Li, Shan, Cheng, Kai-Wen, Wang, Ting Yu, Poh, Yu-Ping, Mazor, Yuval, Liu, Haijun, Chou, Tsui-Fen, Nannenga, Brent L., Chiu, Po-Lin |
| Quelle: | Nature Communications, 13, Art. No. 5824, (2022-10-03) |
| Verlagsinformationen: | Nature Publishing Group |
| Publikationsjahr: | 2022 |
| Bestand: | Caltech Authors (California Institute of Technology) |
| Schlagwörter: | General Physics and Astronomy, General Biochemistry, Genetics and Molecular Biology, General Chemistry, Multidisciplinary |
| Beschreibung: | 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. ; © The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain ... |
| Publikationsart: | article in journal/newspaper |
| Sprache: | unknown |
| Relation: | https://authors.library.caltech.edu/communities/caltechauthors/; https://www.ncbi.nlm.nih.gov/pmc/PMC9529944; eprintid:117493 |
| DOI: | 10.1038/s41467-022-33505-4 |
| Verfügbarkeit: | https://doi.org/10.1038/s41467-022-33505-4 https://www.ncbi.nlm.nih.gov/pmc/PMC9529944 |
| Rights: | info:eu-repo/semantics/closedAccess ; Other |
| Dokumentencode: | edsbas.3DB9C710 |
| Datenbank: | BASE |
Nájsť tento článok vo Web of Science | Abstract: | 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. ; © The Author(s) 2022. This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain ... |
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| DOI: | 10.1038/s41467-022-33505-4 |