3cod

Crystal Structure of T90A/D115A mutant of Bacteriorhodopsin

spinqualitylabelsall models 3cod, resolution 2.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3cod is a 2 chain structure with sequence from "bacillus_halobius_ruber"_klebahn_1919 "bacillus halobius ruber" klebahn 1919. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: RET Related: 1py6, 1xji, 3coc Gene: bop ("Bacillus halobius ruber" Klebahn 1919) Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function [BACR_HALSA] Light-driven proton pump. 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 Understanding the energetics of molecular interactions is fundamental to all of the central quests of structural biology including structure prediction and design, mapping evolutionary pathways, learning how mutations cause disease, drug design, and relating structure to function. Hydrogen-bonding is widely regarded as an important force in a membrane environment because of the low dielectric constant of membranes and a lack of competition from water. Indeed, polar residue substitutions are the most common disease-causing mutations in membrane proteins. Because of limited structural information and technical challenges, however, there have been few quantitative tests of hydrogen-bond strength in the context of large membrane proteins. Here we show, by using a double-mutant cycle analysis, that the average contribution of eight interhelical side-chain hydrogen-bonding interactions throughout bacteriorhodopsin is only 0.6 kcal mol(-1). In agreement with these experiments, we find that 4% of polar atoms in the non-polar core regions of membrane proteins have no hydrogen-bond partner and the lengths of buried hydrogen bonds in soluble proteins and membrane protein transmembrane regions are statistically identical. Our results indicate that most hydrogen-bond interactions in membrane proteins are only modestly stabilizing. Weak hydrogen-bonding should be reflected in considerations of membrane protein folding, dynamics, design, evolution and function. Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins.,Joh NH, Min A, Faham S, Whitelegge JP, Yang D, Woods VL, Bowie JU Nature. 2008 Jun 26;453(7199):1266-70. Epub 2008 May 25. PMID:18500332 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin

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