{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Tani K"],"funding":["MEXT | Japan Society for the Promotion of Science"],"pagination":["1904"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8991256"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["13(1)"],"pubmed_abstract":["Rhodobacter sphaeroides is a model organism in bacterial photosynthesis, and its light-harvesting-reaction center (LH1-RC) complex contains both dimeric and monomeric forms. Here we present cryo-EM structures of the native LH1-RC dimer and an LH1-RC monomer lacking protein-U (ΔU). The native dimer reveals several asymmetric features including the arrangement of its two monomeric components, the structural integrity of protein-U, the overall organization of LH1, and rigidities of the proteins and pigments. PufX plays a critical role in connecting the two monomers in a dimer, with one PufX interacting at its N-terminus with another PufX and an LH1 β-polypeptide in the other monomer. One protein-U was only partially resolved in the dimeric structure, signaling different degrees of disorder in the two monomers. The ΔU LH1-RC monomer was half-moon-shaped and contained 11 α- and 10 β-polypeptides, indicating a critical role for protein-U in controlling the number of αβ-subunits required for dimer assembly and stabilization. These features are discussed in relation to membrane topology and an assembly model proposed for the native dimeric complex."],"journal":["Nature communications"],"pubmed_title":["Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex."],"pmcid":["PMC8991256"],"funding_grant_id":["JP20H05086","JP20H02856"],"pubmed_authors":["Nagashima KVP","Hall M","Wang-Otomo ZY","Kimura Y","Kikuchi R","Takahashi A","Humbel BM","Kawamura S","Kanno R","Tani K","Mizoguchi A","Yu LJ","Madigan MT"],"additional_accession":[]},"is_claimable":false,"name":"Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex.","description":"Rhodobacter sphaeroides is a model organism in bacterial photosynthesis, and its light-harvesting-reaction center (LH1-RC) complex contains both dimeric and monomeric forms. Here we present cryo-EM structures of the native LH1-RC dimer and an LH1-RC monomer lacking protein-U (ΔU). The native dimer reveals several asymmetric features including the arrangement of its two monomeric components, the structural integrity of protein-U, the overall organization of LH1, and rigidities of the proteins and pigments. PufX plays a critical role in connecting the two monomers in a dimer, with one PufX interacting at its N-terminus with another PufX and an LH1 β-polypeptide in the other monomer. One protein-U was only partially resolved in the dimeric structure, signaling different degrees of disorder in the two monomers. The ΔU LH1-RC monomer was half-moon-shaped and contained 11 α- and 10 β-polypeptides, indicating a critical role for protein-U in controlling the number of αβ-subunits required for dimer assembly and stabilization. These features are discussed in relation to membrane topology and an assembly model proposed for the native dimeric complex.","dates":{"release":"2022-01-01T00:00:00Z","publication":"2022 Apr","modification":"2026-05-30T15:28:00.421Z","creation":"2025-04-04T10:02:04.123Z"},"accession":"S-EPMC8991256","cross_references":{"pubmed":["35393413"],"doi":["10.1038/s41467-022-29453-8"]}}