{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["120(5)"],"submitter":["Xie H"],"pubmed_abstract":["Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the Fenna-Matthews-Olson (FMO) proteins to a homodimeric reaction center (RC). Here, we report the cryogenic electron microscopic structure of the intact FMO-RC apparatus from <i>Chlorobaculum tepidum</i> at 2.5 Å resolution. The FMO-RC apparatus presents an asymmetric architecture and contains two FMO trimers that show different interaction patterns with the RC core. Furthermore, the two permanently bound transmembrane subunits PscC, which donate electrons to the special pair, interact only with the two large PscA subunits. This structure fills an important gap in our understanding of the transfer of "],"journal":["Proceedings of the National Academy of Sciences of the United States of America"],"pagination":["e2216734120"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC9945994"],"repository":["biostudies-literature"],"pubmed_title":["Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium <i>Chlorobaculum tepidum</i>."],"pmcid":["PMC9945994"],"pubmed_authors":["Michel H","Lyratzakis A","Xie H","Khera R","Welsch S","Tsiotis G","Koutantou M"],"additional_accession":[]},"is_claimable":false,"name":"Cryo-EM structure of the whole photosynthetic reaction center apparatus from the green sulfur bacterium <i>Chlorobaculum tepidum</i>.","description":"Light energy absorption and transfer are very important processes in photosynthesis. In green sulfur bacteria light is absorbed primarily by the chlorosomes and its energy is transferred via the Fenna-Matthews-Olson (FMO) proteins to a homodimeric reaction center (RC). Here, we report the cryogenic electron microscopic structure of the intact FMO-RC apparatus from <i>Chlorobaculum tepidum</i> at 2.5 Å resolution. The FMO-RC apparatus presents an asymmetric architecture and contains two FMO trimers that show different interaction patterns with the RC core. Furthermore, the two permanently bound transmembrane subunits PscC, which donate electrons to the special pair, interact only with the two large PscA subunits. This structure fills an important gap in our understanding of the transfer of ","dates":{"release":"2023-01-01T00:00:00Z","publication":"2023 Jan","modification":"2026-05-29T01:46:32.839Z","creation":"2025-04-07T03:29:48.797Z"},"accession":"S-EPMC9945994","cross_references":{"pubmed":["36693097"],"doi":["10.1073/pnas.2216734120"]}}