6oop: Difference between revisions

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'''Unreleased structure'''


The entry 6oop is ON HOLD  until Paper Publication
==protein B==
<StructureSection load='6oop' size='340' side='right'caption='[[6oop]], [[Resolution|resolution]] 2.80&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6oop]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillus_coli"_migula_1895 "bacillus coli" migula 1895]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OOP OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OOP FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=KHJ:1,1-dimethyl-4,4-bipyridin-1-ium'>KHJ</scene>, <scene name='pdbligand=PR:PRASEODYMIUM+ION'>PR</scene></td></tr>
<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">A9R57_05385, BJJ90_17655 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=562 "Bacillus coli" Migula 1895])</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6oop FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6oop OCA], [http://pdbe.org/6oop PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6oop RCSB], [http://www.ebi.ac.uk/pdbsum/6oop PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6oop ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
MdfA is a prototypical H(+)-coupled multidrug transporter that is characterized by extraordinarily broad substrate specificity. The involvement of specific H-bonds in MdfA-drug interactions and the simplicity of altering the substrate specificity of MdfA contradict the promiscuous nature of multidrug recognition, presenting a baffling conundrum. Here we show the X-ray structures of MdfA variant I239T/G354E in complexes with three electrically different ligands, determined at resolutions up to 2.2 A. Our structures reveal that I239T/G354E interacts with these compounds differently from MdfA and that I239T/G354E possesses two discrete, non-overlapping substrate-binding sites. Our results shed new light on the molecular design of multidrug-binding and protonation sites and highlight the importance of often-neglected, long-range charge-charge interactions in multidrug recognition. Beyond helping to solve the ostensible conundrum of multidrug recognition, our findings suggest the mechanistic difference between substrate and inhibitor for any H(+)-dependent multidrug transporter, which may open new vistas on curtailing efflux-mediated multidrug resistance.


Authors: Lu, M.
Structure of an engineered multidrug transporter MdfA reveals the molecular basis for substrate recognition.,Wu HH, Symersky J, Lu M Commun Biol. 2019 Jun 17;2:210. doi: 10.1038/s42003-019-0446-y. eCollection 2019. PMID:31240248<ref>PMID:31240248</ref>


Description: protein B
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6oop" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bacillus coli migula 1895]]
[[Category: Large Structures]]
[[Category: Lu, M]]
[[Category: Lu, M]]
[[Category: Complex]]
[[Category: Transport]]
[[Category: Transport protein]]
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