7p03: Difference between revisions

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-'''Unreleased structure'''
-The entry 7p03 is ON HOLD  until Paper Publication
+==Cryo-EM structure of Pdr5 from Saccharomyces cerevisiae in inward-facing conformation without nucleotides==
+<StructureSection load='7p03' size='340' side='right'caption='[[7p03]], [[Resolution|resolution]] 3.45&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7P03 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7P03 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]] 3.45&#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=7p03 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7p03 OCA], [https://pdbe.org/7p03 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7p03 RCSB], [https://www.ebi.ac.uk/pdbsum/7p03 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7p03 ProSAT]</span></td></tr>
+</table>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Pdr5, a member of the extensive ABC transporter superfamily, is representative of a clinically relevant subgroup involved in pleiotropic drug resistance. Pdr5 and its homologues drive drug efflux through uncoupled hydrolysis of nucleotides, enabling organisms such as baker's yeast and pathogenic fungi to survive in the presence of chemically diverse antifungal agents. Here, we present the molecular structure of Pdr5 solved with single particle cryo-EM, revealing details of an ATP-driven conformational cycle, which mechanically drives drug translocation through an amphipathic channel, and a clamping switch within a conserved linker loop that acts as a nucleotide sensor. One half of the transporter remains nearly invariant throughout the cycle, while its partner undergoes changes that are transmitted across inter-domain interfaces to support a peristaltic motion of the pumped molecule. The efflux model proposed here rationalises the pleiotropic impact of Pdr5 and opens new avenues for the development of effective antifungal compounds.
-Authors:
+Structure and efflux mechanism of the yeast pleiotropic drug resistance transporter Pdr5.,Harris A, Wagner M, Du D, Raschka S, Nentwig LM, Gohlke H, Smits SHJ, Luisi BF, Schmitt L Nat Commun. 2021 Sep 6;12(1):5254. doi: 10.1038/s41467-021-25574-8. PMID:34489436<ref>PMID:34489436</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 7p03" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[ABC transporter 3D structures|ABC transporter 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Large Structures]]
+[[Category: Du D]]
+[[Category: Luisi BF]]
+[[Category: Schmitt L]]
+[[Category: Szewczak-Harris A]]
+[[Category: Wagner M]]