8B64
Cryo-EM structure of RC-LH1-PufX photosynthetic core complex from Rba. capsulatus
Summary for 8B64
| Entry DOI | 10.2210/pdb8b64/pdb |
| EMDB information | 15862 |
| Descriptor | Light-harvesting protein B-870 alpha chain, UBIQUINONE-10, 1,2-Distearoyl-sn-glycerophosphoethanolamine, ... (12 entities in total) |
| Functional Keywords | pufx, core complex, rc-lh1, rba capsulatus, photosynthetic core, photosynthesis |
| Biological source | Rhodobacter capsulatus More |
| Total number of polymer chains | 34 |
| Total formula weight | 341138.17 |
| Authors | Bracun, L.,Yamagata, A.,Shirouzu, M.,Liu, L.N. (deposition date: 2022-09-26, release date: 2023-02-01, Last modification date: 2024-07-24) |
| Primary citation | Bracun, L.,Yamagata, A.,Christianson, B.M.,Shirouzu, M.,Liu, L.N. Cryo-EM structure of a monomeric RC-LH1-PufX supercomplex with high-carotenoid content from Rhodobacter capsulatus. Structure, 31:318-, 2023 Cited by 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 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. PubMed: 36738736DOI: 10.1016/j.str.2023.01.006 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.589 Å) |
Structure validation
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