4lz6

</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=4lz6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4lz6 OCA], [https://pdbe.org/4lz6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4lz6 RCSB], [https://www.ebi.ac.uk/pdbsum/4lz6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4lz6 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Multidrug and toxic compound extrusion (MATE) transporters contribute to multidrug resistance by coupling the efflux of drugs to the influx of Na(+) or H(+). Known structures of Na(+)-coupled, extracellular-facing MATE transporters from the NorM subfamily revealed 12 membrane-spanning segments related by a quasi-two-fold rotational symmetry and a multidrug-binding cavity situated near the membrane surface. Here we report the crystal structure of an H(+)-coupled MATE transporter from Bacillus halodurans and the DinF subfamily at 3.2-A resolution, unveiling a surprisingly asymmetric arrangement of 12 transmembrane helices. We also identified a membrane-embedded substrate-binding chamber by combining crystallographic and biochemical analyses. Our studies further suggested a direct competition between H(+) and substrate during DinF-mediated transport and implied how a MATE transporter alternates between its extracellular- and intracellular-facing conformations to propel multidrug extrusion. Collectively, our results demonstrated heretofore-unrecognized mechanistic diversity among MATE transporters.

Structural insights into H(+)-coupled multidrug extrusion by a MATE transporter.,Lu M, Radchenko M, Symersky J, Nie R, Guo Y Nat Struct Mol Biol. 2013 Nov;20(11):1310-7. doi: 10.1038/nsmb.2687. Epub 2013, Oct 20. PMID:24141706<ref>PMID:24141706</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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== References ==

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