1r2n: Difference between revisions
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
|DOMAIN= | |||
|RELATEDENTRY=[[1brr|1BRR]], [[1c3w|1c3w]], [[1qhj|1qhj]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1r2n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r2n OCA], [http://www.ebi.ac.uk/pdbsum/1r2n PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1r2n RCSB]</span> | |||
}} | }} | ||
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[[Category: Simon, B.]] | [[Category: Simon, B.]] | ||
[[Category: terLaak, A.]] | [[Category: terLaak, A.]] | ||
[[Category: haloarchaea]] | [[Category: haloarchaea]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
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[[Category: retinal protein]] | [[Category: retinal protein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:22:23 2008'' | ||
Revision as of 23:22, 30 March 2008
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| Related: | 1BRR, 1c3w, 1qhj
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR structure of the all-trans retinal in dark-adapted Bacteriorhodopsin
OverviewOverview
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.
About this StructureAbout this Structure
1R2N is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
ReferenceReference
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
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