6qwr
From Proteopedia
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| - | '''Unreleased structure''' | ||
| - | + | ==Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers== | |
| + | <StructureSection load='6qwr' size='340' side='right'caption='[[6qwr]]' scene=''> | ||
| + | == Structural highlights == | ||
| + | <table><tr><td colspan='2'>[[6qwr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Pseudomonas_oleovorans Pseudomonas oleovorans]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6QWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6QWR FirstGlance]. <br> | ||
| + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solid-state NMR</td></tr> | ||
| + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6qwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qwr OCA], [https://pdbe.org/6qwr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6qwr RCSB], [https://www.ebi.ac.uk/pdbsum/6qwr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6qwr ProSAT]</span></td></tr> | ||
| + | </table> | ||
| + | == Function == | ||
| + | [https://www.uniprot.org/uniprot/ALKL_PSEOL ALKL_PSEOL] Could be involved in the transport of substrates. | ||
| + | <div style="background-color:#fffaf0;"> | ||
| + | == Publication Abstract from PubMed == | ||
| + | The protein AlkL is known to increase permeability of the outer membrane of bacteria for hydrophobic molecules, yet the mechanism of transport has not been determined. Differing crystal and NMR structures of homologous proteins resulted in a controversy regarding the degree of structure and the role of long extracellular loops. Here we solve this controversy by determining the de novo NMR structure in near-native lipid bilayers, and by accessing structural dynamics relevant to hydrophobic substrate permeation through molecular-dynamics simulations and by characteristic NMR relaxation parameters. Dynamic lateral exit sites large enough to accommodate substrates such as carvone or octane occur through restructuring of a barrel extension formed by the extracellular loops. | ||
| - | + | A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL.,Schubeis T, Le Marchand T, Daday C, Kopec W, Tekwani Movellan K, Stanek J, Schwarzer TS, Castiglione K, de Groot BL, Pintacuda G, Andreas LB Proc Natl Acad Sci U S A. 2020 Aug 19. pii: 2002598117. doi:, 10.1073/pnas.2002598117. PMID:32817429<ref>PMID:32817429</ref> | |
| - | + | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |
| - | [[Category: | + | </div> |
| - | [[Category: | + | <div class="pdbe-citations 6qwr" style="background-color:#fffaf0;"></div> |
| - | [[Category: Andreas | + | == References == |
| - | [[Category: Pintacuda | + | <references/> |
| + | __TOC__ | ||
| + | </StructureSection> | ||
| + | [[Category: Large Structures]] | ||
| + | [[Category: Pseudomonas oleovorans]] | ||
| + | [[Category: Andreas LB]] | ||
| + | [[Category: Pintacuda G]] | ||
| + | [[Category: Schubeis T]] | ||
Current revision
Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers
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