6idr

<StructureSection load='6idr' size='340' side='right' caption='[[6idr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>

<table><tr><td colspan='2'>[[6idr]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/"bacillo_virgola_del_koch"_trevisan_1884 "bacillo virgola del koch" trevisan 1884]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6IDR OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6IDR FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=OLC:(2R)-2,3-DIHYDROXYPROPYL+(9Z)-OCTADEC-9-ENOATE'>OLC</scene></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">CGT79_05080 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=666 "Bacillo virgola del Koch" Trevisan 1884])</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=6idr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6idr OCA], [http://pdbe.org/6idr PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6idr RCSB], [http://www.ebi.ac.uk/pdbsum/6idr PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6idr ProSAT]</span></td></tr>

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== Publication Abstract from PubMed ==

Multidrug and toxic compound extrusion (MATE) transporters efflux toxic compounds using a Na(+) or H(+) gradient across the membrane. Although the structures of MATE transporters have been reported, the cation-coupled substrate transport mechanism remains controversial. Here we report crystal structures of VcmN, a Vibrio cholerae MATE transporter driven by the H(+) gradient. High-resolution structures in two distinct conformations associated with different pHs revealed that the rearrangement of the hydrogen-bonding network around the conserved Asp35 induces the bending of transmembrane helix 1, as in the case of the H(+)-coupled Pyrococcus furiosus MATE transporter. We also determined the crystal structure of the D35N mutant, which captured a unique conformation of TM1 facilitated by an altered hydrogen-bonding network. Based on the present results, we propose a common step in the transport cycle shared among prokaryotic H(+)-coupled MATE transporters.

Structural Basis of H(+)-Dependent Conformational Change in a Bacterial MATE Transporter.,Kusakizako T, Claxton DP, Tanaka Y, Maturana AD, Kuroda T, Ishitani R, Mchaourab HS, Nureki O Structure. 2018 Oct 30. pii: S0969-2126(18)30365-4. doi:, 10.1016/j.str.2018.10.004. PMID:30449688<ref>PMID:30449688</ref>

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

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<div class="pdbe-citations 6idr" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Bacillo virgola del koch trevisan 1884]]

[[Category: Claxton, D P]]

[[Category: Ishitani, R]]

[[Category: Kuroda, T]]

[[Category: Kusakizako, T]]

[[Category: Maturana, A D]]

[[Category: Mchaourab, H S]]

[[Category: Nureki, O]]

[[Category: Tanaka, Y]]

[[Category: Transport protein]]