2hg3

Reaction centre from Rhodobacter sphaeroides strain R-26.1 complexed with brominated phosphatidylcholine

spinqualitylabelsall models 2hg3, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2hg3 is a 3 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: X-ray diffraction, Resolution 2.7Å Ligands: BPH, CDL, FE, GOL, HTO, K, LDA, PC9, PO4, U10 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RCEL_CERSP 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 This study describes the use of brominated phospholipids to distinguish between lipid and detergent binding sites on the surface of a typical alpha-helical membrane protein. Reaction centers isolated from Rhodobacter sphaeroides were cocrystallized with added brominated phospholipids. X-ray structural analysis of these crystals has revealed the presence of two lipid binding sites from the characteristic strong X-ray scattering from the bromine atoms. These results demonstrate the usefulness of this approach to mapping lipid binding sites at the surface of membrane proteins. Brominated lipids identify lipid binding sites on the surface of the reaction center from Rhodobacter sphaeroides.,Roszak AW, Gardiner AT, Isaacs NW, Cogdell RJ Biochemistry. 2007 Mar 20;46(11):2909-16. Epub 2007 Feb 23. PMID:17315985 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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