3mkt

<StructureSection load='3mkt' size='340' side='right' caption='[[3mkt]], [[Resolution|resolution]] 3.65&Aring;' scene=''>

<table><tr><td colspan='2'>[[3mkt]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Vibch Vibch]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3MKT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3MKT FirstGlance]. <br>

</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3mku|3mku]]</td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">NorM ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=243277 VIBCH])</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=3mkt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3mkt OCA], [http://pdbe.org/3mkt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3mkt RCSB], [http://www.ebi.ac.uk/pdbsum/3mkt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3mkt ProSAT]</span></td></tr>

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Transporter proteins from the MATE (multidrug and toxic compound extrusion) family are vital in metabolite transport in plants, directly affecting crop yields worldwide. MATE transporters also mediate multiple-drug resistance (MDR) in bacteria and mammals, modulating the efficacy of many pharmaceutical drugs used in the treatment of a variety of diseases. MATE transporters couple substrate transport to electrochemical gradients and are the only remaining class of MDR transporters whose structure has not been determined. Here we report the X-ray structure of the MATE transporter NorM from Vibrio cholerae determined to 3.65 A, revealing an outward-facing conformation with two portals open to the outer leaflet of the membrane and a unique topology of the predicted 12 transmembrane helices distinct from any other known MDR transporter. We also report a cation-binding site in close proximity to residues previously deemed critical for transport. This conformation probably represents a stage of the transport cycle with high affinity for monovalent cations and low affinity for substrates.

Structure of a cation-bound multidrug and toxic compound extrusion transporter.,He X, Szewczyk P, Karyakin A, Evin M, Hong WX, Zhang Q, Chang G Nature. 2010 Oct 21;467(7318):991-4. Epub 2010 Sep 22. PMID:20861838<ref>PMID:20861838</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 3mkt" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Vibch]]

[[Category: Chang, G]]

[[Category: Evin, M]]

[[Category: He, X]]

[[Category: Hong, W X]]

[[Category: Karyakin, A]]

[[Category: Szewczyk, P]]

[[Category: Zhang, Q]]

[[Category: Transport protein]]