6idr: Difference between revisions

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'''Unreleased structure'''


The entry 6idr is ON HOLD
==Crystal structure of Vibrio cholerae MATE transporter VcmN in the bent form==
<StructureSection load='6idr' size='340' side='right' caption='[[6idr]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[6idr]] is a 1 chain structure. 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='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>
</table>
<div style="background-color:#fffaf0;">
== 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.


Authors:  
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>


Description:  
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
<div class="pdbe-citations 6idr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[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: Mate multidrug transporter]]
[[Category: Transport protein]]
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