ArticlePhilosophical transactions of the Royal Society of London. Series B, Biological sciences2012
Structure of the dimeric RC-LH1-PufX complex from Rhodobaca bogoriensis investigated by electron microscopy.
Article in Philosophical transactions of the Royal Society of London. Series B, Biological sciences, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed.
- 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
- Differential stability of bacterial photosynthetic apparatus ofFrontiers in microbiology · 2024Article
- 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
- A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex.Nature communications · 2021Article
- A comparative look at structural variation among RC-LH1 'Core' complexes present in anoxygenic phototrophic bacteria.Photosynthesis research · 2020Review
- Variation in supramolecular organisation of the photosynthetic membrane of Rhodobacter sphaeroides induced by alteration of PufX.Photosynthesis research · 2014Article
- Integrating current knowledge in various aspects of thylakoid membrane structure and dynamics.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Article
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5 authors.
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Abstract
Electron microscopy and single-particle averaging were performed on isolated reaction centre (RC)-antenna complexes (RC-LH1-PufX complexes) of Rhodobaca bogoriensis strain LBB1, with the aim of establishing the LH1 antenna conformation, and, in particular, the structural role of the PufX protein. Projection maps of dimeric complexes were obtained at 13 Å resolution and show the positions of the 2 × 14 LH1 α- and β-subunits. This new dimeric complex displays two open, C-shaped LH1 aggregates of 13 αβ polypeptides partially surrounding the RCs plus two LH1 units forming the dimer interface in the centre. Between the interface and the two half rings are two openings on each side. Next to the openings, there are four additional densities present per dimer, considered to be occupied by four copies of PufX. The position of the RC in our model was verified by comparison with RC-LH1-PufX complexes in membranes. Our model differs from previously proposed configurations for Rhodobacter species in which the LH1 ribbon is continuous in the shape of an S, and the stoichiometry is of one PufX per RC.
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