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1vjm
From Proteopedia
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| - | [[Image:1vjm.gif|left|200px]] | + | [[Image:1vjm.gif|left|200px]] |
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| - | '''Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin''' | + | {{Structure |
| + | |PDB= 1vjm |SIZE=350|CAPTION= <scene name='initialview01'>1vjm</scene>, resolution 2.3Å | ||
| + | |SITE= | ||
| + | |LIGAND= <scene name='pdbligand=RET:RETINAL'>RET</scene> | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1VJM is a [ | + | 1VJM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_sp. Halobacterium sp.]. This structure supersedes the now removed PDB entry 1R3P. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJM OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/14532280 14532280] |
[[Category: Halobacterium sp.]] | [[Category: Halobacterium sp.]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:46:30 2008'' |
Revision as of 12:46, 20 March 2008
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| 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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