9rsj

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'''Unreleased structure'''
 
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The entry 9rsj is ON HOLD until Paper Publication
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==Cryo-EM structure of MATE transporter NorM-VC in complex with doxorubicin==
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<StructureSection load='9rsj' size='340' side='right'caption='[[9rsj]], [[Resolution|resolution]] 3.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[9rsj]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Lama_glama Lama glama], [https://en.wikipedia.org/wiki/Vibrio_cholerae Vibrio cholerae] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=9RSJ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9RSJ FirstGlance]. <br>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 3.1&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=DM2:DOXORUBICIN'>DM2</scene></td></tr>
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=9rsj FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9rsj OCA], [https://pdbe.org/9rsj PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9rsj RCSB], [https://www.ebi.ac.uk/pdbsum/9rsj PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9rsj ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/C3LML9_VIBCM C3LML9_VIBCM]
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Multidrug and toxic compound extrusion (MATE) transport proteins contribute to multidrug resistance in human pathogens by extruding various cytotoxic compounds from the cellular interior. Despite their importance across all domains of life, the specificities and mechanisms of substrate transport of these proteins remain poorly understood due to limited structural and functional information. Here, we determined the cryo-electron microscopy structure of NorM from Vibrio cholerae (NorM-VC) in complex with the anthracycline antibiotic doxorubicin, using the NabFab approach. The structure reveals that the doxorubicin-binding pocket is located halfway through the membrane, within the C-lobe of the protein. Functional studies targeting the doxorubicin-interacting residues validated the binding pocket and enabled detailed analysis of the doxorubicin transport reaction. Our findings indicate doxorubicin binding within a multisite binding chamber engaged in a general transport mechanism for a variety of substrates.
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Authors:
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Doxorubicin recognition and transport by the MATE multidrug transporter NorM from Vibrio cholerae.,Hsieh PY, Romane K, Kowal J, Locher KP, van Veen HW J Mol Biol. 2025 Nov 17:169549. doi: 10.1016/j.jmb.2025.169549. PMID:41260293<ref>PMID:41260293</ref>
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Description:
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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<div class="pdbe-citations 9rsj" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Lama glama]]
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[[Category: Large Structures]]
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[[Category: Synthetic construct]]
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[[Category: Vibrio cholerae]]
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[[Category: Hsieh PY]]
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[[Category: Kowal J]]
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[[Category: Locher KP]]
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[[Category: Romane K]]
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[[Category: Van Veen HW]]

Current revision

Cryo-EM structure of MATE transporter NorM-VC in complex with doxorubicin

PDB ID 9rsj

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