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Title | Cryo-EM structure of a monomeric RC-LH1-PufX supercomplex with high-carotenoid content from Rhodobacter capsulatus. |
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Journal, issue, pages | Structure, Vol. 31, Issue 3, Page 318-328.e3, Year 2023 |
Publish date | Mar 2, 2023 |
Authors | Laura Bracun / Atsushi Yamagata / Bern M Christianson / Mikako Shirouzu / Lu-Ning Liu / |
PubMed Abstract | In purple photosynthetic bacteria, the photochemical reaction center (RC) and light-harvesting complex 1 (LH1) assemble to form monomeric or dimeric RC-LH1 membrane complexes, essential for bacterial ...In purple photosynthetic bacteria, the photochemical reaction center (RC) and light-harvesting complex 1 (LH1) assemble to form monomeric or dimeric RC-LH1 membrane complexes, essential for bacterial photosynthesis. Here, we report a 2.59-Å resolution cryoelectron microscopy (cryo-EM) structure of the RC-LH1 supercomplex from Rhodobacter capsulatus. We show that Rba. capsulatus RC-LH1 complexes are exclusively monomers in which the RC is surrounded by a 15-subunit LH1 ring. Incorporation of a transmembrane polypeptide PufX leads to a large opening within the LH1 ring. Each LH1 subunit associates two carotenoids and two bacteriochlorophylls, which is similar to Rba. sphaeroides RC-LH1 but more than one carotenoid per LH1 in Rba. veldkampii RC-LH1 monomer. Collectively, the unique Rba. capsulatus RC-LH1-PufX represents an intermediate structure between Rba. sphaeroides and Rba. veldkampii RC-LH1-PufX. Comparison of PufX from the three Rhodobacter species indicates the important residues involved in dimerization of RC-LH1. |
External links | Structure / PubMed:36738736 |
Methods | EM (single particle) |
Resolution | 2.589 Å |
Structure data | EMDB-15862, PDB-8b64: |
Chemicals | ChemComp-BCL: ChemComp-SPO: ChemComp-BPH: ChemComp-U10: ChemComp-3PE: ChemComp-FE: |
Source |
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Keywords | PHOTOSYNTHESIS / PufX / core complex / RC-LH1 / Rba capsulatus / photosynthetic core |