View source for 5ng5


==multi-drug efflux; membrane transport; RND superfamily; Drug resistance==
<SX load='5ng5' size='340' side='right' viewer='molstar' caption='[[5ng5]], [[Resolution|resolution]] 6.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5ng5]] is a 15 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5NG5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5NG5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 6.5&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=5QF:6-[2-(3,4-DIMETHOXYPHENYL)ETHYLSULFANYL]-8-[4-(2-METHOXYETHYL)PIPERAZIN-1-YL]-3,3-DIMETHYL-1,4-DIHYDROPYRANO[3,4-C]PYRIDINE-5-CARBONITRILE'>5QF</scene></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=5ng5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5ng5 OCA], [https://pdbe.org/5ng5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5ng5 RCSB], [https://www.ebi.ac.uk/pdbsum/5ng5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5ng5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/ACRA_ECOLI ACRA_ECOLI] AcrA-AcrB-AcrZ-TolC is a drug efflux protein complex with broad substrate specificity that uses the proton motive force to export substrates. This subunit may act as an adapter protein that links AcrB and TolC stably together. It is elongated in shape, being long enough to span the periplasm.<ref>PMID:9878415</ref> 
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== Publication Abstract from PubMed ==
Bacterial efflux pumps confer multidrug resistance by transporting diverse antibiotics from the cell. In Gram-negative bacteria, some of these pumps form multi-protein assemblies that span the cell envelope. Here we report the near-atomic resolution cryoEM structures of the Escherichia coli AcrAB-TolC multidrug efflux pump in resting and drug transport states, revealing a quaternary structural switch that allosterically couples and synchronizes initial ligand binding with channel opening. Within the transport-activated state, the channel remains open even though the pump cycles through three distinct conformations. Collectively, our data provide a dynamic mechanism for the assembly and operation of the AcrAB-TolC pump.

An allosteric transport mechanism for the AcrAB-TolC Multidrug Efflux Pump.,Wang Z, Fan G, Hryc CF, Blaza JN, Serysheva II, Schmid MF, Chiu W, Luisi BF, Du D Elife. 2017 Mar 29;6. pii: e24905. doi: 10.7554/eLife.24905. PMID:28355133<ref>PMID:28355133</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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<div class="pdbe-citations 5ng5" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</SX>
[[Category: Escherichia coli]]
[[Category: Large Structures]]
[[Category: Blaza JN]]
[[Category: Chiu W]]
[[Category: Du D]]
[[Category: Fan G]]
[[Category: Hryc CF]]
[[Category: Luisi BF]]
[[Category: Schmid MF]]
[[Category: Serysheva II]]
[[Category: Wang Z]]