1pxs

Structure of Met56Ala mutant of Bacteriorhodopsin

spinqualitylabelsall models 1pxs, resolution 2.20Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1pxs 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: 1pxr, 1py6 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 The molecular forces that stabilize membrane protein structure are poorly understood. To investigate these forces we introduced alanine substitutions at 24 positions in the B helix of bacteriorhodopsin and examined their effects on structure and stability. Although most of the results can be rationalized in terms of the folded structure, there are a number of surprises. (1) We find a remarkably high frequency of stabilizing mutations (17%), indicating that membrane proteins are not highly optimized for stability. (2) Helix B is kinked, with the kink centered around Pro50. The P50A mutation has no effect on stability, however, and a crystal structure reveals that the helix remains bent, indicating that tertiary contacts dominate in the distortion of this helix. (3) We find that the protein is stabilized by about 1kcal/mol for every 38A(2) of surface area buried, which is quite similar to soluble proteins in spite of their dramatically different environments. (4) We find little energetic difference, on average, in the burial of apolar surface or polar surface area, implying that van der Waals packing is the dominant force that drives membrane protein folding. Side-chain contributions to membrane protein structure and stability.,Faham S, Yang D, Bare E, Yohannan S, Whitelegge JP, Bowie JU J Mol Biol. 2004 Jan 2;335(1):297-305. PMID:14659758 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin 3D structures

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