5c6n

</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=5c6n FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6n OCA], [https://pdbe.org/5c6n PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6n RCSB], [https://www.ebi.ac.uk/pdbsum/5c6n PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6n ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Multidrug and toxic compound extrusion (MATE) transporters underpin multidrug resistance by using the H(+) or Na(+) electrochemical gradient to extrude different drugs across cell membranes. MATE transporters can be further parsed into the DinF, NorM and eukaryotic subfamilies based on their amino-acid sequence similarity. Here we report the 3.0 A resolution X-ray structures of a protonation-mimetic mutant of an H(+)-coupled DinF transporter, as well as of an H(+)-coupled DinF and a Na(+)-coupled NorM transporters in complexes with verapamil, a small-molecule pharmaceutical that inhibits MATE-mediated multidrug extrusion. Combining structure-inspired mutational and functional studies, we confirm the biological relevance of our crystal structures, reveal the mechanistic differences among MATE transporters, and suggest how verapamil inhibits MATE-mediated multidrug efflux. Our findings offer insights into how MATE transporters extrude chemically and structurally dissimilar drugs and could inform the design of new strategies for tackling multidrug resistance.

Structural basis for the blockade of MATE multidrug efflux pumps.,Radchenko M, Symersky J, Nie R, Lu M Nat Commun. 2015 Aug 6;6:7995. doi: 10.1038/ncomms8995. PMID:26246409<ref>PMID:26246409</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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