View source for 6hfb


==Outward-facing conformation of a multidrug resistance MATE family transporter of the MOP superfamily.==
<StructureSection load='6hfb' size='340' side='right'caption='[[6hfb]], [[Resolution|resolution]] 3.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6hfb]] is a 4 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6HFB OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6HFB FirstGlance]. <br>
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CS:CESIUM+ION'>CS</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=6hfb FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6hfb OCA], [http://pdbe.org/6hfb PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6hfb RCSB], [http://www.ebi.ac.uk/pdbsum/6hfb PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6hfb ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Multidrug and toxic compound extrusion (MATE) transporters mediate excretion of xenobiotics and toxic metabolites, thereby conferring multidrug resistance in bacterial pathogens and cancer cells. Structural information on the alternate conformational states and knowledge of the detailed mechanism of MATE transport are of great importance for drug development. However, the structures of MATE transporters are only known in V-shaped outward-facing conformations. Here, we present the crystal structure of a MATE transporter from Pyrococcus furiosus (PfMATE) in the long-sought-after inward-facing state, which was obtained after crystallization in the presence of native lipids. Transition from the outward-facing state to the inward-facing state involves rigid body movements of transmembrane helices (TMs) 2-6 and 8-12 to form an inverted V, facilitated by a loose binding of TM1 and TM7 to their respective bundles and their conformational flexibility. The inward-facing structure of PfMATE in combination with the outward-facing one supports an alternating access mechanism for the MATE family transporters.

Inward-facing conformation of a multidrug resistance MATE family transporter.,Zakrzewska S, Mehdipour AR, Malviya VN, Nonaka T, Koepke J, Muenke C, Hausner W, Hummer G, Safarian S, Michel H Proc Natl Acad Sci U S A. 2019 Jun 3. pii: 1904210116. doi:, 10.1073/pnas.1904210116. PMID:31160466<ref>PMID:31160466</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 6hfb" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Michel, H]]
[[Category: Nonaka, T]]
[[Category: Safarian, S]]
[[Category: Zakrzewska, S]]
[[Category: Membrane protein]]
[[Category: Transporter]]