6rqo
From Proteopedia
(Difference between revisions)
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| - | '''Unreleased structure''' | ||
| - | + | ==Steady-state-SMX activated state structure of bacteriorhodopsin== | |
| + | <StructureSection load='6rqo' size='340' side='right'caption='[[6rqo]], [[Resolution|resolution]] 2.00Å' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6rqo]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Halobacterium_salinarum_(strain_atcc_700922_/_jcm_11081_/_nrc-1) Halobacterium salinarum (strain atcc 700922 / jcm 11081 / nrc-1)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6RQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6RQO FirstGlance]. <br> | ||
| + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=RET:RETINAL'>RET</scene></td></tr> | ||
| + | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6rnj|6rnj]], [[6rph|6rph]]</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=6rqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6rqo OCA], [http://pdbe.org/6rqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6rqo RCSB], [http://www.ebi.ac.uk/pdbsum/6rqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6rqo ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [[http://www.uniprot.org/uniprot/BACR_HALSA BACR_HALSA]] Light-driven proton pump. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | Conformational dynamics are essential for proteins to function. We adapted time-resolved serial crystallography developed at x-ray lasers to visualize protein motions using synchrotrons. We recorded the structural changes in the light-driven proton-pump bacteriorhodopsin over 200 milliseconds in time. The snapshot from the first 5 milliseconds after photoactivation shows structural changes associated with proton release at a quality comparable to that of previous x-ray laser experiments. From 10 to 15 milliseconds onwards, we observe large additional structural rearrangements up to 9 angstroms on the cytoplasmic side. Rotation of leucine-93 and phenylalanine-219 opens a hydrophobic barrier, leading to the formation of a water chain connecting the intracellular aspartic acid-96 with the retinal Schiff base. The formation of this proton wire recharges the membrane pump with a proton for the next cycle. | ||
| - | + | Proton uptake mechanism in bacteriorhodopsin captured by serial synchrotron crystallography.,Weinert T, Skopintsev P, James D, Dworkowski F, Panepucci E, Kekilli D, Furrer A, Brunle S, Mous S, Ozerov D, Nogly P, Wang M, Standfuss J Science. 2019 Jul 5;365(6448):61-65. doi: 10.1126/science.aaw8634. PMID:31273117<ref>PMID:31273117</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| + | <div class="pdbe-citations 6rqo" style="background-color:#fffaf0;"></div> | ||
| + | == References == | ||
| + | <references/> | ||
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Bruenle, S]] | ||
| + | [[Category: Furrer, A]] | ||
| + | [[Category: James, D]] | ||
| + | [[Category: Kekilli, D]] | ||
| + | [[Category: Mous, S]] | ||
| + | [[Category: Nogly, P]] | ||
| + | [[Category: Skopintsev, P]] | ||
| + | [[Category: Standfuss, J]] | ||
| + | [[Category: Weinert, T]] | ||
| + | [[Category: Proton transport]] | ||
| + | [[Category: Retinal]] | ||
| + | [[Category: Serial crystallography]] | ||
| + | [[Category: Time-resolved crystallography]] | ||
| + | [[Category: Tr-smx]] | ||
Revision as of 10:52, 17 July 2019
Steady-state-SMX activated state structure of bacteriorhodopsin
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