1f50

BACTERIORHODOPSIN-BR STATE OF THE E204Q MUTANT AT 1.7 ANGSTROM RESOLUTION

spinqualitylabelsall models 1f50, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1f50 is a 1 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: LI1, RET, SQU Related: 1c3w, 1c8r, 1c8s, 1f4z 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 In order to understand how isomerization of the retinal drives unidirectional transmembrane ion transport in bacteriorhodopsin, we determined the atomic structures of the BR state and M photointermediate of the E204Q mutant, to 1.7 and 1.8 A resolution, respectively. Comparison of this M, in which proton release to the extracellular surface is blocked, with the previously determined M in the D96N mutant indicates that the changes in the extracellular region are initiated by changes in the electrostatic interactions of the retinal Schiff base with Asp85 and Asp212, but those on the cytoplasmic side originate from steric conflict of the 13-methyl retinal group with Trp182 and distortion of the pi-bulge of helix G. The structural changes suggest that protonation of Asp85 initiates a cascade of atomic displacements in the extracellular region that cause release of a proton to the surface. The progressive relaxation of the strained 13-cis retinal chain with deprotonated Schiff base, in turn, initiates atomic displacements in the cytoplasmic region that cause the intercalation of a hydrogen-bonded water molecule between Thr46 and Asp96. This accounts for the lowering of the pK(a) of Asp96, which then reprotonates the Schiff base via a newly formed chain of water molecules that is extending toward the Schiff base. Coupling photoisomerization of retinal to directional transport in bacteriorhodopsin.,Luecke H, Schobert B, Cartailler JP, Richter HT, Rosengarth A, Needleman R, Lanyi JK J Mol Biol. 2000 Jul 28;300(5):1237-55. PMID:10903866 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin 3D structures

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