5y50: Difference between revisions

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'''Unreleased structure'''


The entry 5y50 is ON HOLD  until Paper Publication
==Crystal structure of eukaryotic MATE transporter AtDTX14==
<StructureSection load='5y50' size='340' side='right'caption='[[5y50]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5y50]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5Y50 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5Y50 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</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=5y50 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5y50 OCA], [https://pdbe.org/5y50 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5y50 RCSB], [https://www.ebi.ac.uk/pdbsum/5y50 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5y50 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/DTX14_ARATH DTX14_ARATH]
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Mulitidrug and toxic compound extrusion (MATE) family transporters export xenobiotics to maintain cellular homeostasis. The human MATE transporters mediate the excretion of xenobiotics and cationic clinical drugs, whereas some plant MATE transporters are responsible for aluminum tolerance and secondary metabolite transport. Here we report the crystal structure of the eukaryotic MATE transporter from Arabidopsis thaliana, at 2.6 A resolution. The structure reveals that its carboxy-terminal lobe (C-lobe) contains an extensive hydrogen-bonding network with well-conserved acidic residues, and their importance is demonstrated by the structure-based mutational analysis. The structural and functional analyses suggest that the transport mechanism involves the structural change of transmembrane helix 7, induced by the formation of a hydrogen-bonding network upon the protonation of the conserved acidic residue in the C-lobe. Our findings provide insights into the transport mechanism of eukaryotic MATE transporters, which is important for the improvement of the pharmacokinetics of the clinical drugs.


Authors: Miyauchi, H., Kusakizako, T., Nishizawa, T., Ishitani, R., Nureki, O.
Structural basis for xenobiotic extrusion by eukaryotic MATE transporter.,Miyauchi H, Moriyama S, Kusakizako T, Kumazaki K, Nakane T, Yamashita K, Hirata K, Dohmae N, Nishizawa T, Ito K, Miyaji T, Moriyama Y, Ishitani R, Nureki O Nat Commun. 2017 Nov 21;8(1):1633. doi: 10.1038/s41467-017-01541-0. PMID:29158478<ref>PMID:29158478</ref>


Description: Crystal structure of a protein
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
[[Category: Unreleased Structures]]
</div>
[[Category: Nureki, O]]
<div class="pdbe-citations 5y50" style="background-color:#fffaf0;"></div>
[[Category: Miyauchi, H]]
== References ==
[[Category: Nishizawa, T]]
<references/>
[[Category: Ishitani, R]]
__TOC__
[[Category: Kusakizako, T]]
</StructureSection>
[[Category: Arabidopsis thaliana]]
[[Category: Large Structures]]
[[Category: Ishitani R]]
[[Category: Kusakizako T]]
[[Category: Miyauchi H]]
[[Category: Nishizawa T]]
[[Category: Nureki O]]
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