1vjm
From Proteopedia
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|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vjm FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vjm OCA], [http://www.ebi.ac.uk/pdbsum/1vjm PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vjm RCSB]</span> | ||
}} | }} | ||
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[[Category: Spoel, D van der.]] | [[Category: Spoel, D van der.]] | ||
[[Category: Taylor, T.]] | [[Category: Taylor, T.]] | ||
- | [[Category: RET]] | ||
[[Category: hydrogen ion transport]] | [[Category: hydrogen ion transport]] | ||
[[Category: ion transport]] | [[Category: ion transport]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:25:22 2008'' |
Revision as of 21:25, 30 March 2008
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, resolution 2.3Å | |||||||
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Ligands: | |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin
Overview
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.
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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