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| | ==Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers== | | ==Solid-state NMR structure of outer membrane protein AlkL in DMPC lipid bilayers== |
| - | <StructureSection load='6qwr' size='340' side='right'caption='[[6qwr]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='6qwr' size='340' side='right'caption='[[6qwr]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6qwr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_17440_[[pseudomonas_pseudoalcaligenes]] Atcc 17440 [[pseudomonas pseudoalcaligenes]]]. 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 [http://proteopedia.org/fgij/fg.htm?mol=6QWR FirstGlance]. <br> | + | <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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[6qam|6qam]]</td></tr> | + | </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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">alkL ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=301 ATCC 17440 [[Pseudomonas pseudoalcaligenes]]])</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> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6qwr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6qwr OCA], [http://pdbe.org/6qwr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6qwr RCSB], [http://www.ebi.ac.uk/pdbsum/6qwr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6qwr ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ALKL_PSEOL ALKL_PSEOL]] Could be involved in the transport of substrates. | + | [https://www.uniprot.org/uniprot/ALKL_PSEOL ALKL_PSEOL] Could be involved in the transport of substrates. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Andreas, L B]] | + | [[Category: Pseudomonas oleovorans]] |
| - | [[Category: Pintacuda, G]] | + | [[Category: Andreas LB]] |
| - | [[Category: Schubeis, T]] | + | [[Category: Pintacuda G]] |
| - | [[Category: Beta barrel]] | + | [[Category: Schubeis T]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Outer membrane protein]]
| + | |
| - | [[Category: Porin]]
| + | |
| - | [[Category: Transporter]]
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| Structural highlights
Function
ALKL_PSEOL Could be involved in the transport of substrates.
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ 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. A beta-barrel for oil transport through lipid membranes: Dynamic NMR structures of AlkL. Proc Natl Acad Sci U S A. 2020 Aug 19. pii: 2002598117. doi:, 10.1073/pnas.2002598117. PMID:32817429 doi:http://dx.doi.org/10.1073/pnas.2002598117
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