ArticleNature communications2021
A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex.
Article in Nature communications, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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Who cites it
20 citing papers in PubMed, 41 citations in OpenAlex.
- Molecular dissection of the Cereibacter sphaeroides spheroidene monooxygenase.The Biochemical journal · 2026Article
- Structural insights into the photochemistry of the LH1-RC complex from the marine purple phototrophic bacterium Rhodovulum sulfidophilum.Communications biology · 2026Article
- Article
- Structural basis for aerobic anoxygenic photosynthesis in the reaction center-light-harvesting 1 (RC-LH1) supercomplex of Dinoroseobacter shibae.Communications biology · 2025Article
- Molecular and structural insights into neurosporene accumulation in Rhodobacter sphaeroides G1C.Photosynthesis research · 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
- Living Therapeutics for Synergistic Hydrogen-Photothermal Cancer Treatment by Photosynthetic Bacteria.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2025Article
- Insights into the divergence of the photosynthetic LH1 complex obtained from structural analysis of the unusual photocomplexes of Roseospirillum parvum.Communications biology · 2024Article
- Tunneling Mechanisms of Quinones in Photosynthetic Reaction Center-Light Harvesting 1 Supercomplexes.Small science · 2024Article
- Architectures of photosynthetic RC-LH1 supercomplexes fromScience advances · 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
- Rhodobacter capsulatus forms a compact crescent-shaped LH1-RC photocomplex.Nature communications · 2023Article
- The role of the γ subunit in the photosystem of the lowest-energy phototrophs.The Biochemical journal · 2022Article
- An LH1-RC photocomplex from an extremophilic phototroph provides insight into origins of two photosynthesis proteins.Communications biology · 2022Article
- A CaThe Journal of biological chemistry · 2022Article
- Structural basis for the assembly and quinone transport mechanisms of the dimeric photosynthetic RC-LH1 supercomplex.Nature communications · 2022Article
- Asymmetric structure of the native Rhodobacter sphaeroides dimeric LH1-RC complex.Nature communications · 2022Article
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Authors and funding
12 authors at 7 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Rhodobacter (Rba.) sphaeroides is the most widely used model organism in bacterial photosynthesis. The light-harvesting-reaction center (LH1-RC) core complex of this purple phototroph is characterized by the co-existence of monomeric and dimeric forms, the presence of the protein PufX, and approximately two carotenoids per LH1 αβ-polypeptides. Despite many efforts, structures of the Rba. sphaeroides LH1-RC have not been obtained at high resolutions. Here we report a cryo-EM structure of the monomeric LH1-RC from Rba. sphaeroides strain IL106 at 2.9 Å resolution. The LH1 complex forms a C-shaped structure composed of 14 αβ-polypeptides around the RC with a large ring opening. From the cryo-EM density map, a previously unrecognized integral membrane protein, referred to as protein-U, was identified. Protein-U has a U-shaped conformation near the LH1-ring opening and was annotated as a hypothetical protein in the Rba. sphaeroides genome. Deletion of protein-U resulted in a mutant strain that expressed a much-reduced amount of the dimeric LH1-RC, indicating an important role for protein-U in dimerization of the LH1-RC complex. PufX was located opposite protein-U on the LH1-ring opening, and both its position and conformation differed from that of previous reports of dimeric LH1-RC structures obtained at low-resolution. Twenty-six molecules of the carotenoid spheroidene arranged in two distinct configurations were resolved in the Rba. sphaeroides LH1 and were positioned within the complex to block its channels. Our findings offer an exciting new view of the core photocomplex of Rba. sphaeroides and the connections between structure and function in bacterial photocomplexes in general.
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