1bm1: Difference between revisions
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPG:PHOSPHORIC+ACID+2,3-BIS-(3,7,11,15-TETRAMETHYL-HEXADECYLOXY)-PROPYL+ESTER+2-HYDROXO-3-PHOSPHONOOXY-PROPYL+ESTER'>DPG</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DPG:PHOSPHORIC+ACID+2,3-BIS-(3,7,11,15-TETRAMETHYL-HEXADECYLOXY)-PROPYL+ESTER+2-HYDROXO-3-PHOSPHONOOXY-PROPYL+ESTER'>DPG</scene>, <scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
<tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></td></tr> | <tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=PCA:PYROGLUTAMIC+ACID'>PCA</scene></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=1bm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm1 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1bm1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bm1 PDBsum]</span></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=1bm1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bm1 OCA], [http://pdbe.org/1bm1 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1bm1 RCSB], [http://www.ebi.ac.uk/pdbsum/1bm1 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1bm1" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
Revision as of 22:08, 10 September 2015
CRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATECRYSTAL STRUCTURE OF BACTERIORHODOPSIN IN THE LIGHT-ADAPTED STATE
Structural highlights
Function[BACR_HALSA] Light-driven proton pump. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedIn the purple membrane of Halobacterium salinarium, bacteriorhodopsin trimers are arranged in a hexagonal lattice. When purple membrane sheets are incubated at high temperature with neutral detergent, membrane vesicularization takes place, yielding inside-out vesicles with a diameter of 50 nm. The vesicular structure becomes unstable at low temperature, where successive fusion of the vesicles yields a crystal which is composed of stacked planar membranes. X-ray crystallographic analysis reveals that the bacteriorhodopsin trimers are arranged in a honeycomb lattice in each membrane layer and that neighbouring membranes orient in opposite directions. The native structure of the trimeric unit is preserved in the honeycomb lattice, irrespective of alterations in the in-plane orientation of the trimer. One phospholipid tightly bound to a crevice between monomers in the trimeric unit is suggested to act as a glue in the formation of the trimer. Specific lipid-protein interactions in a novel honeycomb lattice structure of bacteriorhodopsin.,Sato H, Takeda K, Tani K, Hino T, Okada T, Nakasako M, Kamiya N, Kouyama T Acta Crystallogr D Biol Crystallogr. 1999 Jul;55(Pt 7):1251-6. PMID:10393291[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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