1vjm

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{{STRUCTURE_1vjm| PDB=1vjm | SCENE= }}
{{STRUCTURE_1vjm| PDB=1vjm | SCENE= }}
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'''Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin'''
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===Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin===
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==Overview==
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X-ray and electron diffraction studies of specific reaction intermediates, or reaction intermediate analogues, have produced a consistent picture of the structural mechanism of light-driven proton pumping by bacteriorhodopsin. Of central importance within this picture is the structure of the L-intermediate, which follows the retinal all-trans to 13-cis photoisomerization step of the K-intermediate and sets the stage for the primary proton transfer event from the positively charged Schiff base to the negatively charged Asp-85. Here we report the structural changes in bacteriorhodopsin following red light illumination at 150 K. Single crystal microspectrophotometry showed that only the L-intermediate is populated in three-dimensional crystals under these conditions. The experimental difference Fourier electron density map and refined crystallographic structure were consistent with those previously presented (Royant, A., Edman, K., Ursby, T., Pebay-Peyroula, E., Landau, E. M., and Neutze, R. (2000) Nature 406, 645-648; Royant, A., Edman, K., Ursby, T., Pebay-Peyroula, E., Landau, E. M., and Neutze, R. (2001) Photochem. Photobiol. 74, 794-804). Based on the refined crystallographic structures, molecular dynamic simulations were used to examine the influence of the conformational change of the protein that is associated with the K-to-L transition on retinal dynamics. Implications regarding the structural mechanism for proton pumping by bacteriorhodopsin are discussed.
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==About this Structure==
==About this Structure==
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[[Category: Retinal protein]]
[[Category: Retinal protein]]
[[Category: Transmembrane]]
[[Category: Transmembrane]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jul 10 12:36:30 2008''

Revision as of 09:36, 10 July 2008

Image:1vjm.png

Template:STRUCTURE 1vjm

Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin

Template:ABSTRACT PUBMED 14532280

About this Structure

1VJM is a Single protein structure of sequence from Halobacterium sp.. This structure supersedes the now removed PDB entry 1r3p. Full crystallographic information is available from OCA.

Reference

Deformation of helix C in the low temperature L-intermediate of bacteriorhodopsin., Edman K, Royant A, Larsson G, Jacobson F, Taylor T, van der Spoel D, Landau EM, Pebay-Peyroula E, Neutze R, J Biol Chem. 2004 Jan 16;279(3):2147-58. Epub 2003 Oct 7. PMID:14532280

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