7f0l

STRUCTURE OF PHOTOSYNTHETIC LH1-RC SUPER-COMPLEX OF RHODOBACTER SPHAEROIDES MONOMER

spinqualitylabelsall models 7f0l, resolution 2.94Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7f0l is a 33 chain structure with sequence from Cereibacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.94Å Ligands: BPH, CDL, FE, FME, LDA, LMT, PGV, SPO, U10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RCEL_CERS4 The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. Publication Abstract from PubMed 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 alphabeta-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 A resolution. The LH1 complex forms a C-shaped structure composed of 14 alphabeta-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. A previously unrecognized membrane protein in the Rhodobacter sphaeroides LH1-RC photocomplex.,Tani K, Nagashima KVP, Kanno R, Kawamura S, Kikuchi R, Hall M, Yu LJ, Kimura Y, Madigan MT, Mizoguchi A, Humbel BM, Wang-Otomo ZY Nat Commun. 2021 Nov 2;12(1):6300. doi: 10.1038/s41467-021-26561-9. PMID:34728609 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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