1r2n | pdb_00001r2n

NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin

spinqualitylabelsall models 1r2n, 12 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1r2n is a 1 chain structure with sequence from Halobacterium salinarium. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: RET Related: 1brr, 1c3w, 1qhj 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 two forms of bacteriorhodopsin present in the dark-adapted state, containing either all-trans or 13-cis,15-syn retinal, were examined by using solution state NMR, and their structures were determined. Comparison of the all-trans and the 13-cis,15-syn forms shows a shift in position of about 0.25 A within the pocket of the protein. Comparing this to the 13-cis,15-anti chromophore of the catalytic cycle M-intermediate structure, the 13-cis,15-syn form demonstrates a less pronounced up-tilt of the retinal C12[bond]C14 region, while leaving W182 and T178 essentially unchanged. The N[bond]H dipole of the Schiff base orients toward the extracellular side in both forms, however, it reorients toward the intracellular side in the 13-cis,15-anti configuration to form the catalytic M-intermediate. Thus, the change of the N[bond]H dipole is considered primarily responsible for energy storage, conformation changes of the protein, and the deprotonation of the Schiff base. The structural similarity of the all-trans and 13-cis,15-syn forms is taken as strong evidence for the ion dipole dragging model by which proton (hydroxide ion) translocation follows the change of the dipole. The structures of the active center in dark-adapted bacteriorhodopsin by solution-state NMR spectroscopy.,Patzelt H, Simon B, terLaak A, Kessler B, Kuhne R, Schmieder P, Oesterhelt D, Oschkinat H Proc Natl Acad Sci U S A. 2002 Jul 23;99(15):9765-70. Epub 2002 Jul 15. PMID:12119389 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Bacteriorhodopsin 3D structures

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