6t1z

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Current revision (07:38, 1 May 2024) (edit) (undo)
 
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<StructureSection load='6t1z' size='340' side='right'caption='[[6t1z]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
<StructureSection load='6t1z' size='340' side='right'caption='[[6t1z]], [[Resolution|resolution]] 2.90&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
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<table><tr><td colspan='2'>[[6t1z]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacterium_lactis"_lister_1873 "bacterium lactis" lister 1873]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T1Z OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6T1Z FirstGlance]. <br>
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<table><tr><td colspan='2'>[[6t1z]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Lactococcus_lactis Lactococcus lactis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6T1Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6T1Z FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HT1:2-(4-ETHOXYPHENYL)-5-(4-METHYL-1-PIPERAZINYL)-2,5-BI-BENZIMIDAZOLE'>HT1</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=XP4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE'>XP4</scene></td></tr>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.9&#8491;</td></tr>
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<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">lmrP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=1358 "Bacterium lactis" Lister 1873])</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=HT1:2-(4-ETHOXYPHENYL)-5-(4-METHYL-1-PIPERAZINYL)-2,5-BI-BENZIMIDAZOLE'>HT1</scene>, <scene name='pdbligand=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</scene>, <scene name='pdbligand=XP4:1,2-DIMYRISTOYL-SN-GLYCERO-3-PHOSPHATE'>XP4</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6t1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1z OCA], [http://pdbe.org/6t1z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6t1z RCSB], [http://www.ebi.ac.uk/pdbsum/6t1z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1z ProSAT]</span></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=6t1z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6t1z OCA], [https://pdbe.org/6t1z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6t1z RCSB], [https://www.ebi.ac.uk/pdbsum/6t1z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6t1z ProSAT]</span></td></tr>
</table>
</table>
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<div style="background-color:#fffaf0;">
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== Function ==
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== Publication Abstract from PubMed ==
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[https://www.uniprot.org/uniprot/Q48658_9LACT Q48658_9LACT]
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Multidrug efflux pumps present a challenge to the treatment of bacterial infections, making it vitally important to understand their mechanism of action. Here, we investigate the nature of substrate binding within Lactococcus lactis LmrP, a prototypical multidrug transporter of the major facilitator superfamily. We determined the crystal structure of LmrP in a ligand-bound outward-open state and observed an embedded lipid in the binding cavity of LmrP, an observation supported by native mass spectrometry analyses. Molecular dynamics simulations suggest that the anionic lipid stabilizes the observed ligand-bound structure. Mutants engineered to disrupt binding of the embedded lipid display reduced transport of some, but not all, antibiotic substrates. Our results suggest that a lipid within the binding cavity could provide a malleable hydrophobic component that allows adaptation to the presence of different substrates, helping to explain the broad specificity of this protein and possibly other multidrug transporters.
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An embedded lipid in the multidrug transporter LmrP suggests a mechanism for polyspecificity.,Debruycker V, Hutchin A, Masureel M, Ficici E, Martens C, Legrand P, Stein RA, Mchaourab HS, Faraldo-Gomez JD, Remaut H, Govaerts C Nat Struct Mol Biol. 2020 Jul 27. pii: 10.1038/s41594-020-0464-y. doi:, 10.1038/s41594-020-0464-y. PMID:32719456<ref>PMID:32719456</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 6t1z" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
__TOC__
</StructureSection>
</StructureSection>
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[[Category: Bacterium lactis lister 1873]]
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[[Category: Lactococcus lactis]]
[[Category: Large Structures]]
[[Category: Large Structures]]
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[[Category: Debruycker, V]]
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[[Category: Debruycker V]]
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[[Category: Govaerts, C]]
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[[Category: Govaerts C]]
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[[Category: Hutchin, A]]
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[[Category: Hutchin A]]
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[[Category: Legrand, P]]
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[[Category: Legrand P]]
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[[Category: Masureel, M]]
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[[Category: Masureel M]]
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[[Category: Remaut, H]]
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[[Category: Remaut H]]
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[[Category: Transmembrane multidrug transporter]]
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[[Category: Transport protein]]
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Current revision

LmrP from L. lactis, in an outward-open conformation, bound to Hoechst 33342

PDB ID 6t1z

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OCA

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