6ooq

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'''Unreleased structure'''
 
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The entry 6ooq is ON HOLD until Paper Publication
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==protein C==
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<StructureSection load='6ooq' size='340' side='right'caption='[[6ooq]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[6ooq]] 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=6OOQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6OOQ FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=DXC:(3ALPHA,5BETA,12ALPHA)-3,12-DIHYDROXYCHOLAN-24-OIC+ACID'>DXC</scene></td></tr>
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<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>
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<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=6ooq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ooq OCA], [http://pdbe.org/6ooq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ooq RCSB], [http://www.ebi.ac.uk/pdbsum/6ooq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ooq ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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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.
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Authors: Lu, M.
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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>
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Description: protein C
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 6ooq" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bacillus coli migula 1895]]
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[[Category: Large Structures]]
[[Category: Lu, M]]
[[Category: Lu, M]]
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[[Category: Complex]]
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[[Category: Transport protein]]

Revision as of 11:54, 1 January 2020

protein C

PDB ID 6ooq

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