ArticleNature communications2022
Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex.
Article in Nature communications, 2022. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 38 citations in OpenAlex.
- Molecular dissection of the Cereibacter sphaeroides spheroidene monooxygenase.The Biochemical journal · 2026Article
- Minimization of Disorder as a Key Design Principle for Natural Sizes of Light Harvesting 2 Complexes.The journal of physical chemistry letters · 2026Article
- Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum.Communications biology · 2026Article
- Structural basis for aerobic anoxygenic photosynthesis in the reaction center-light-harvesting 1 (RC-LH1) supercomplex of Dinoroseobacter shibae.Communications biology · 2025Article
- Cyanobacterial redox carriers support photosynthesis in a purple phototrophic bacterium.The Biochemical journal · 2025Article
- Cryo-EM Analysis of a Tri-Heme Cytochrome-Associated RC-LH1 Complex from the Marine Photoheterotrophic Bacterium Dinoroseobacter Shibae.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- A distinct double-ring LH1-LH2 photocomplex from an extremophilic phototroph.Nature communications · 2025Article
- Genomic highlights of the phylogenetically unique halophilic purple nonsulfur bacterium, Rhodothalassium salexigens.Extremophiles : life under extreme conditions · 2025Article
- The potential correlations between cell-free extracts fromFood chemistry: X · 2024Article
- Insights into the divergence of the photosynthetic LH1 complex obtained from structural analysis of the unusual photocomplexes of Roseospirillum parvum.Communications biology · 2024Article
- Architectures of photosynthetic RC-LH1 supercomplexes fromScience advances · 2024Article
- Sulfoquinovosyl diacylglycerol is required for dimerisation of the Rhodobacter sphaeroides reaction centre-light harvesting 1 core complex.The Biochemical journal · 2024Article
- Excitation energy transfer in proteoliposomes reconstituted with LH2 and RC-LH1 complexes from Rhodobacter sphaeroides.Bioscience reports · 2024Article
- Article
- Genomic basis for the unique phenotype of the alkaliphilic purple nonsulfur bacterium Rhodobaca bogoriensis.Extremophiles : life under extreme conditions · 2023Article
- The structure and assembly of reaction centre-light-harvesting 1 complexes in photosynthetic bacteria.Bioscience reports · 2023Article
- Cryo-EM structure of the four-subunitProceedings of the National Academy of Sciences of the United States of America · 2023Article
- Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex.Nature communications · 2023Article
- An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.Communications biology · 2022Article
- Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex.Nature communications · 2022Article
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Authors and funding
13 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
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.
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