1rg5 | pdb_00001rg5

Structure of the photosynthetic reaction centre from Rhodobacter sphaeroides carotenoidless strain R-26.1

spinqualitylabelsall models 1rg5, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1rg5 is a 3 chain structure with sequence from Rhodobacter sphaeroides. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCL, BPH, CDL, FE, HTO, LDA, U10 Related: 4rcr, 1rgn, 1rqk Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RCEL_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEH_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEM_RHOSH] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed X-ray diffraction was used to determine high-resolution structures of the reaction center (RC) complex from the carotenoidless mutant, Rb. sphaeroides R-26.1, without or reconstituted with carotenoids. The results are compared with the structure of the RC from a semiaerobically grown Rb. sphaeroides strain 2.4.1. The investigation reveals the structure of the carotenoid in the different protein preparations, the nature of its binding site, and a plausible mechanism by which the carotenoid is incorporated unidirectionally in its characteristic geometric configuration. The structural data suggest that the accessibility of the carotenoid to the binding site is controlled by a specific "gatekeeper" residue which allows the carotenoid to approach the binding site from only one direction. Carotenoid binding to the protein is secured by hydrogen bonding to a separate "locking" amino acid. The study reveals the specific molecular interactions that control how the carotenoid protects the photosynthetic apparatus against photo-induced oxidative destruction. Protein regulation of carotenoid binding; gatekeeper and locking amino acid residues in reaction centers of Rhodobacter sphaeroides.,Roszak AW, McKendrick K, Gardiner AT, Mitchell IA, Isaacs NW, Cogdell RJ, Hashimoto H, Frank HA Structure. 2004 May;12(5):765-73. PMID:15130469 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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