View source for 7szt


==Crystal structure of Gdx-Clo from Small Multidrug Resistance family of transporters in low pH (protonated state)==
<StructureSection load='7szt' size='340' side='right'caption='[[7szt]], [[Resolution|resolution]] 2.32&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7szt]] is a 8 chain structure with sequence from [https://en.wikipedia.org/wiki/Clostridiales_bacterium_oral_taxon_876 Clostridiales bacterium oral taxon 876] 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=7SZT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7SZT 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]] 2.32&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9PD:Dodecyldimethylphosphine+oxide'>9PD</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=7szt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7szt OCA], [https://pdbe.org/7szt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7szt RCSB], [https://www.ebi.ac.uk/pdbsum/7szt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7szt ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/U2EQ00_9FIRM U2EQ00_9FIRM] 
<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 7szt" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Clostridiales bacterium oral taxon 876]]
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Burata OE]]
[[Category: Kermani AA]]
[[Category: Stockbridge RB]]