4mt1

</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=4mt1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4mt1 OCA], [https://pdbe.org/4mt1 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4mt1 RCSB], [https://www.ebi.ac.uk/pdbsum/4mt1 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4mt1 ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Active efflux of antimicrobial agents is one of the most important strategies used by bacteria to defend against antimicrobial factors present in their environment. Mediating many cases of antibiotic resistance are transmembrane efflux pumps, composed of one or more proteins. The Neisseria gonorrhoeae MtrCDE tripartite multidrug efflux pump, belonging to the hydrophobic and amphiphilic efflux resistance-nodulation-cell division (HAE-RND) family, spans both the inner and outer membranes of N. gonorrhoeae and confers resistance to a variety of antibiotics and toxic compounds. We here describe the crystal structure of N. gonorrhoeae MtrE, the outer membrane component of the MtrCDE tripartite multidrug efflux system. This trimeric MtrE channel forms a vertical tunnel extending down contiguously from the outer membrane surface to the periplasmic end, indicating that our structure of MtrE depicts an open conformational state of this channel.

Crystal structure of the open state of the Neisseria gonorrhoeae MtrE outer membrane channel.,Lei HT, Chou TH, Su CC, Bolla JR, Kumar N, Radhakrishnan A, Long F, Delmar JA, Do SV, Rajashankar KR, Shafer WM, Yu EW PLoS One. 2014 Jun 5;9(6):e97475. doi: 10.1371/journal.pone.0097475. eCollection , 2014. PMID:24901251<ref>PMID:24901251</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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