View source for 7ssu


==Structure of EmrE-D3 mutant in complex with monobody L10 and methyltriphenylphosphonium==
<StructureSection load='7ssu' size='340' side='right'caption='[[7ssu]], [[Resolution|resolution]] 3.22&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7ssu]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7SSU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SSU FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3.22&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=B5J:methyltriphenylphosphonium'>B5J</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=7ssu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7ssu OCA], [https://pdbe.org/7ssu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7ssu RCSB], [https://www.ebi.ac.uk/pdbsum/7ssu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7ssu ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/EMRE_ECOLI EMRE_ECOLI] Multidrug transporter that expels positively charged hydrophobic drugs across the inner membrane of E.coli., thereby conferring resistance to a wide range of toxic compounds. The drug efflux is coupled to an influx of protons. Is involved in the resistance of E.coli cells to methyl viologen, ethidium bromide and acriflavine. Is also able to transport tetraphenylphosphonium (TPP(+)) and benzalkonium.<ref>PMID:7896833</ref> <ref>PMID:10681497</ref> <ref>PMID:15371426</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Proteins from the bacterial small multidrug resistance (SMR) family are proton-coupled exporters of diverse antiseptics and antimicrobials, including polyaromatic cations and quaternary ammonium compounds. The transport mechanism of the Escherichia coli transporter, EmrE, has been studied extensively, but a lack of high-resolution structural information has impeded a structural description of its molecular mechanism. Here, we apply a novel approach, multipurpose crystallization chaperones, to solve several structures of EmrE, including a 2.9 A structure at low pH without substrate. We report five additional structures in complex with structurally diverse transported substrates, including quaternary phosphonium, quaternary ammonium, and planar polyaromatic compounds. These structures show that binding site tryptophan and glutamate residues adopt different rotamers to conform to disparate structures without requiring major rearrangements of the backbone structure. Structural and functional comparison to Gdx-Clo, an SMR protein that transports a much narrower spectrum of substrates, suggests that in EmrE, a relatively sparse hydrogen bond network among binding site residues permits increased sidechain flexibility.

Crystal structures of bacterial small multidrug resistance transporter EmrE in complex with structurally diverse substrates.,Kermani AA, Burata OE, Koff BB, Koide A, Koide S, Stockbridge RB Elife. 2022 Mar 7;11:e76766. doi: 10.7554/eLife.76766. PMID:35254261<ref>PMID:35254261</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7ssu" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Escherichia coli K-12]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Kermani AA]]
[[Category: Stockbridge RB]]