View source for 9vsw


==Structure of Cdr1 with beauvericin==
<StructureSection load='9vsw' size='340' side='right'caption='[[9vsw]], [[Resolution|resolution]] 2.95&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[9vsw]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Candida_albicans_SC5314 Candida albicans SC5314] 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=9VSW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=9VSW FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.95&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MEA:N-METHYLPHENYLALANINE'>MEA</scene>, <scene name='pdbligand=VAD:DEAMINOHYDROXYVALINE'>VAD</scene></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=9vsw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=9vsw OCA], [https://pdbe.org/9vsw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=9vsw RCSB], [https://www.ebi.ac.uk/pdbsum/9vsw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=9vsw ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/CDR1_CANAL CDR1_CANAL] Pleiotropic ABC efflux transporter that confers resistance to numerous chemicals including anisomycin, cycloheximide, fluconazole, miconazole, ketoconazole, itriconazole, nystatin, terbinafine, amorolfine, brefeldin A, amphotericin B, fluphenazine, as well as estrogen. Plays a role in farnesol-induced apoptotic process through glutathione efflux activity. Mediates in-to-out translocation of membrane phospholipids including aminophospholipids and thus regulates asymmetric distribution of phosphatidylethanolamine. Exhibits nucleoside triphosphatase activity.<ref>PMID:10029989</ref> <ref>PMID:10227177</ref> <ref>PMID:10428921</ref> <ref>PMID:11709310</ref> <ref>PMID:11870854</ref> <ref>PMID:12709320</ref> <ref>PMID:14665469</ref> <ref>PMID:15152937</ref> <ref>PMID:15190023</ref> <ref>PMID:15486081</ref> <ref>PMID:15937063</ref> <ref>PMID:16291868</ref> <ref>PMID:16475832</ref> <ref>PMID:16622073</ref> <ref>PMID:16782311</ref> <ref>PMID:17202662</ref> <ref>PMID:18056285</ref> <ref>PMID:18268086</ref> <ref>PMID:18710914</ref> <ref>PMID:19223631</ref> <ref>PMID:19393219</ref> <ref>PMID:20002912</ref> <ref>PMID:20348384</ref> <ref>PMID:20876623</ref> <ref>PMID:22166216</ref> <ref>PMID:22205973</ref> <ref>PMID:23824183</ref> <ref>PMID:23979757</ref> <ref>PMID:8891134</ref> <ref>PMID:9124851</ref> <ref>PMID:9453158</ref> <ref>PMID:9605504</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
In Candida albicans-a World Health Organization fungal priority pathogen-overexpression of the adenosine triphosphate (ATP)-binding cassette transporter Cdr1 drives multidrug resistance. We present seven cryo-electron microscopy structures capturing substrate entry and expulsion. An inward-facing transmembrane channel with three on-off substrate binding sites defines a proposed entry pathway for a single substrate molecule. Coordinated ATP binding to both nucleotide-binding domains induces transmembrane domain closure, driving the substrate expulsion; adenosine diphosphate release following ATP hydrolysis resets the transporter to an inward-open conformation, enabling substrate entry for the next translocation cycle. Structures with three structurally diverse inhibitors resolve two distinct binding modes: one occupying all three substrate sites and another specifically binding two extracellular-proximal sites. These findings provide snapshots of the substrate translocation cycle and structural blueprints for antifungal drug design.

Cryo-EM structures of Cdr1 reveal snapshots of substrate transport and diverse inhibitor recognition.,Wang Z, Yang S, Zhang B, Jiang H, Li Y, Gao R, Wang Y, Fan F, Dong L, Qiu J, Li X, Zhou Y, Murchie AIH, Yu X Sci Adv. 2026 Aug 28;12(35):eaef7706. doi: 10.1126/sciadv.aef7706. Epub 2026 Aug , 28. PMID:42664345<ref>PMID:42664345</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 9vsw" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Candida albicans SC5314]]
[[Category: Large Structures]]
[[Category: Synthetic construct]]
[[Category: Wang Z]]
[[Category: Yang S]]
[[Category: Yu X]]
[[Category: Zhang B]]