1vjm: Difference between revisions

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[[Image:1vjm.png|left|200px]]
==Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin==
<StructureSection load='1vjm' size='340' side='right' caption='[[1vjm]], [[Resolution|resolution]] 2.30&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1vjm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_sp. Halobacterium sp.]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1r3p 1r3p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJM OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1VJM FirstGlance]. <br>
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene><br>
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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.rcsb.org/pdb/explore.do?structureId=1vjm RCSB], [http://www.ebi.ac.uk/pdbsum/1vjm PDBsum]</span></td></tr>
<table>
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/vj/1vjm_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/chain_selection.php?pdb_ID=2ata ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


{{STRUCTURE_1vjm|  PDB=1vjm  |  SCENE=  }}
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<ref>PMID:14532280</ref>


===Deformation of helix C in the low-temperature L-intermediate of bacteriorhodopsin===
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 
</div>
{{ABSTRACT_PUBMED_14532280}}
 
==About this Structure==
[[1vjm]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_sp. Halobacterium sp.]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1r3p 1r3p]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VJM OCA].


==See Also==
==See Also==
*[[Bacteriorhodopsin|Bacteriorhodopsin]]
*[[Bacteriorhodopsin|Bacteriorhodopsin]]
 
== References ==
==Reference==
<references/>
<ref group="xtra">PMID:014532280</ref><references group="xtra"/>
__TOC__
</StructureSection>
[[Category: Halobacterium sp.]]
[[Category: Halobacterium sp.]]
[[Category: Edman, K.]]
[[Category: Edman, K.]]
Retrieved from "https://proteopedia.org/1vjm"