5c6p: Difference between revisions

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==protein C==
==protein C==
<StructureSection load='5c6p' size='340' side='right' caption='[[5c6p]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='5c6p' size='340' side='right'caption='[[5c6p]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[5c6p]] is a 2 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5C6P FirstGlance]. <br>
<table><tr><td colspan='2'>[[5c6p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] and [https://en.wikipedia.org/wiki/Neisseria_gonorrhoeae_FA_1090 Neisseria gonorrhoeae FA 1090]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5C6P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5C6P FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=4YH:(2S)-2-(3,4-DIMETHOXYPHENYL)-5-{[2-(3,4-DIMETHOXYPHENYL)ETHYL](METHYL)AMINO}-2-(PROPAN-2-YL)PENTANENITRILE'>4YH</scene></td></tr>
</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&#8491;</td></tr>
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5c6o|5c6o]], [[5c6n|5c6n]]</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=4YH:(2S)-2-(3,4-DIMETHOXYPHENYL)-5-{[2-(3,4-DIMETHOXYPHENYL)ETHYL](METHYL)AMINO}-2-(PROPAN-2-YL)PENTANENITRILE'>4YH</scene></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=5c6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6p OCA], [http://pdbe.org/5c6p PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5c6p RCSB], [http://www.ebi.ac.uk/pdbsum/5c6p PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6p ProSAT]</span></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=5c6p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5c6p OCA], [https://pdbe.org/5c6p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5c6p RCSB], [https://www.ebi.ac.uk/pdbsum/5c6p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5c6p ProSAT]</span></td></tr>
</table>
</table>
<div style="background-color:#fffaf0;">
== Function ==
== Publication Abstract from PubMed ==
[https://www.uniprot.org/uniprot/Q5F9J8_NEIG1 Q5F9J8_NEIG1]
Multidrug and toxic compound extrusion (MATE) transporters underpin multidrug resistance by using the H(+) or Na(+) electrochemical gradient to extrude different drugs across cell membranes. MATE transporters can be further parsed into the DinF, NorM and eukaryotic subfamilies based on their amino-acid sequence similarity. Here we report the 3.0 A resolution X-ray structures of a protonation-mimetic mutant of an H(+)-coupled DinF transporter, as well as of an H(+)-coupled DinF and a Na(+)-coupled NorM transporters in complexes with verapamil, a small-molecule pharmaceutical that inhibits MATE-mediated multidrug extrusion. Combining structure-inspired mutational and functional studies, we confirm the biological relevance of our crystal structures, reveal the mechanistic differences among MATE transporters, and suggest how verapamil inhibits MATE-mediated multidrug efflux. Our findings offer insights into how MATE transporters extrude chemically and structurally dissimilar drugs and could inform the design of new strategies for tackling multidrug resistance.
 
Structural basis for the blockade of MATE multidrug efflux pumps.,Radchenko M, Symersky J, Nie R, Lu M Nat Commun. 2015 Aug 6;6:7995. doi: 10.1038/ncomms8995. PMID:26246409<ref>PMID:26246409</ref>
 
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5c6p" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
__TOC__
</StructureSection>
</StructureSection>
[[Category: Lu, M]]
[[Category: Escherichia coli]]
[[Category: Protein]]
[[Category: Large Structures]]
[[Category: Transport protein]]
[[Category: Neisseria gonorrhoeae FA 1090]]
[[Category: Lu M]]

Latest revision as of 12:19, 6 March 2024

protein C

5c6p, resolution 3.00Å

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