1vjm
From Proteopedia
(New page: 200px<br /><applet load="1vjm" size="450" color="white" frame="true" align="right" spinBox="true" caption="1vjm, resolution 2.3Å" /> '''Deformation of helix ...) |
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| - | [[Image:1vjm.gif|left|200px]]<br /><applet load="1vjm" size=" | + | [[Image:1vjm.gif|left|200px]]<br /><applet load="1vjm" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1vjm, resolution 2.3Å" /> | caption="1vjm, resolution 2.3Å" /> | ||
'''Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin'''<br /> | '''Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin'''<br /> | ||
==Overview== | ==Overview== | ||
| - | X-ray and electron diffraction studies of specific reaction intermediates, or reaction intermediate analogues, have produced a consistent picture of | + | 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== | ==About this Structure== | ||
| - | 1VJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_sp. Halobacterium sp.] with RET as [http://en.wikipedia.org/wiki/ligand ligand]. This structure | + | 1VJM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Halobacterium_sp. Halobacterium sp.] with <scene name='pdbligand=RET:'>RET</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. 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== | ||
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[[Category: Edman, K.]] | [[Category: Edman, K.]] | ||
[[Category: Jacobson, F.]] | [[Category: Jacobson, F.]] | ||
| - | [[Category: Landau, E | + | [[Category: Landau, E M.]] |
[[Category: Larsson, G.]] | [[Category: Larsson, G.]] | ||
[[Category: Neutze, R.]] | [[Category: Neutze, R.]] | ||
[[Category: Pebay-Peyroula, E.]] | [[Category: Pebay-Peyroula, E.]] | ||
[[Category: Royant, A.]] | [[Category: Royant, A.]] | ||
| - | [[Category: Spoel, D | + | [[Category: Spoel, D van der.]] |
[[Category: Taylor, T.]] | [[Category: Taylor, T.]] | ||
[[Category: RET]] | [[Category: RET]] | ||
| Line 29: | Line 29: | ||
[[Category: transmembrane]] | [[Category: transmembrane]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:35:59 2008'' |
Revision as of 13:35, 21 February 2008
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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. with as ligand. 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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