1prc | pdb_00001prc

CRYSTALLOGRAPHIC REFINEMENT AT 2.3 ANGSTROMS RESOLUTION AND REFINED MODEL OF THE PHOTOSYNTHETIC REACTION CENTER FROM RHODOPSEUDOMONAS VIRIDIS

spinqualitylabelsall models 1prc, resolution 2.30Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1prc is a 4 chain structure with sequence from Atcc 19567. The October 2001 RCSB PDB Molecule of the Month feature on Photosystem I by David S. Goodsell is 10.2210/rcsb_pdb/mom_2001_10. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: BCB, BPB, FE, HEM, LDA, MQ7, NS1, SO4, UQ1 NonStd Res: FME Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [RCEH_RHOVI] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [CYCR_RHOVI] The reaction center of purple bacteria contains a tightly bound cytochrome molecule which re-reduces the photo oxidized primary electron donor. [RCEM_RHOVI] The reaction center is a membrane-bound complex that mediates the initial photochemical event in the electron transfer process of photosynthesis. [RCEL_RHOVI] 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 The atomic model of the photosynthetic reaction centre from the purple bacterium Rhodopseudomonas viridis has been refined to an R-value of 0.193 at 2.3 A resolution. The refined model contains 10,288 non-hydrogen atoms; 10,045 of these have well defined electron density. A Luzzati-plot indicates an average co-ordinate error of 0.26 A. During refinement, the positions of a partially ordered carotenoid, a unibiquinone in the partially occupied QB site, a detergent molecule, seven putative sulphate ions, and 201 water molecules were found. More than half of these waters are bound at interfaces between protein subunits and therefore contribute significantly to subunit interactions. Water molecules also play important structural and probably functional roles in the environment of some of the cofactors. Two water molecules form hydrogen bonds to the accessory bacteriochlorophylls and to the protein in the vicinity of the special pair of bacteriophylls, the primary electron donor. A group of about 10 water molecules is bound near the binding site of the secondary quinone QB. These waters are likely to participate in the transfer of protons to the doubly reduced QB. Crystallographic refinement at 2.3 A resolution and refined model of the photosynthetic reaction centre from Rhodopseudomonas viridis.,Deisenhofer J, Epp O, Sinning I, Michel H J Mol Biol. 1995 Feb 24;246(3):429-57. PMID:7877166 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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