1r2n
From Proteopedia
| Line 7: | Line 7: | ||
|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> | ||
}} | }} | ||
| Line 30: | Line 33: | ||
[[Category: Simon, B.]] | [[Category: Simon, B.]] | ||
[[Category: terLaak, A.]] | [[Category: terLaak, A.]] | ||
| - | [[Category: RET]] | ||
[[Category: haloarchaea]] | [[Category: haloarchaea]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| Line 39: | Line 41: | ||
[[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 20:22, 30 March 2008
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| Ligands: | |||||||
| 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
Overview
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 Structure
1R2N is a Single protein structure of sequence from Halobacterium salinarum. Full crystallographic information is available from OCA.
Reference
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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