3ns0
From Proteopedia
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| - | [[ | + | ==X-ray structure of bacteriorhodopsin== |
| + | <StructureSection load='3ns0' size='340' side='right' caption='[[3ns0]], [[Resolution|resolution]] 1.78Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[3ns0]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum Halobacterium salinarum]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3NS0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3NS0 FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LI1:1-[2,6,10.14-TETRAMETHYL-HEXADECAN-16-YL]-2-[2,10,14-TRIMETHYLHEXADECAN-16-YL]GLYCEROL'>LI1</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3nsb|3nsb]]</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ns0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ns0 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3ns0 RCSB], [http://www.ebi.ac.uk/pdbsum/3ns0 PDBsum]</span></td></tr> | ||
| + | </table> | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Bacteriorhodopsin (bR) provides light-driven vectorial proton transport across a cell membrane. Creation of electrochemical potential at the membrane is a universal step in energy transformation in a cell. Published atomic crystallographic models of early intermediate states of bR show a significant difference between them, and conclusions about pumping mechanisms have been contradictory. Here, we present a quantitative high-resolution crystallographic study of conformational changes in bR induced by X-ray absorption. It is shown that X-ray doses that are usually accumulated during data collection for intermediate-state studies are sufficient to significantly alter the structure of the protein. X-ray-induced changes occur primarily in the active site of bR. Structural modeling showed that X-ray absorption triggers retinal isomerization accompanied by the disappearance of electron densities corresponding to the water molecule W402 bound to the Schiff base. It is demonstrated that these and other X-ray-induced changes may mimic functional conformational changes of bR leading to misinterpretation of the earlier obtained X-ray crystallographic structures of photointermediates. | ||
| - | + | X-ray-Radiation-Induced Changes in Bacteriorhodopsin Structure.,Borshchevskiy VI, Round ES, Popov AN, Buldt G, Gordeliy VI J Mol Biol. 2011 Apr 21. PMID:21530535<ref>PMID:21530535</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | + | </div> | |
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==See Also== | ==See Also== | ||
*[[Bacteriorhodopsin|Bacteriorhodopsin]] | *[[Bacteriorhodopsin|Bacteriorhodopsin]] | ||
| - | + | == References == | |
| - | == | + | <references/> |
| - | < | + | __TOC__ |
| + | </StructureSection> | ||
[[Category: Halobacterium salinarum]] | [[Category: Halobacterium salinarum]] | ||
| - | [[Category: Borshchevskiy, V I | + | [[Category: Borshchevskiy, V I]] |
[[Category: 7-helix transmembrane]] | [[Category: 7-helix transmembrane]] | ||
[[Category: Ion pump]] | [[Category: Ion pump]] | ||
Revision as of 13:37, 9 December 2014
X-ray structure of bacteriorhodopsin
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