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1r84
From Proteopedia
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[[Image:1r84.jpg|left|200px]] | [[Image:1r84.jpg|left|200px]] | ||
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| - | + | {{STRUCTURE_1r84| PDB=1r84 | SCENE= }} | |
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'''NMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsin''' | '''NMR structure of the 13-cis-15-syn retinal in dark_adapted bacteriorhodopsin''' | ||
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[[Category: Schmieder, P.]] | [[Category: Schmieder, P.]] | ||
[[Category: Simon, B.]] | [[Category: Simon, B.]] | ||
| - | [[Category: | + | [[Category: Haloarchea]] |
| - | [[Category: | + | [[Category: Membrane protein]] |
| - | [[Category: | + | [[Category: Nmr]] |
| - | [[Category: | + | [[Category: Photoreceptor]] |
| - | [[Category: | + | [[Category: Proton pump]] |
| - | [[Category: | + | [[Category: Proton transport]] |
| - | [[Category: | + | [[Category: Retinal protein]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:12:06 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 04:12, 3 May 2008
NMR structure of the 13-cis-15-syn 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
1R84 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 Page seeded by OCA on Sat May 3 07:12:06 2008
