View source for 7qkr


==Cryo-EM structure of ABC transporter STE6-2p from Pichia pastoris with Verapamil at 3.2 A resolution==
<StructureSection load='7qkr' size='340' side='right'caption='[[7qkr]], [[Resolution|resolution]] 3.20&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7qkr]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Komagataella_phaffii_CBS_7435 Komagataella phaffii CBS 7435]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7QKR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7QKR 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]] 3.2&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=9Z9:(3beta,14beta,17beta,25R)-3-[4-methoxy-3-(methoxymethyl)butoxy]spirost-5-en'>9Z9</scene>, <scene name='pdbligand=ANP:PHOSPHOAMINOPHOSPHONIC+ACID-ADENYLATE+ESTER'>ANP</scene>, <scene name='pdbligand=I6H:Dexverapamil'>I6H</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</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=7qkr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7qkr OCA], [https://pdbe.org/7qkr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7qkr RCSB], [https://www.ebi.ac.uk/pdbsum/7qkr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7qkr ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/F2QQK6_KOMPC F2QQK6_KOMPC] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Adenosine triphosphate (ATP)-binding cassette (ABC) transporters are multidomain transmembrane proteins, which facilitate the transport of various substances across cell membranes using energy derived from ATP hydrolysis. They are important drug targets since they mediate decreased drug susceptibility during pharmacological treatments. For the methylotrophic yeast Pichia pastoris, a model organism that is a widely used host for protein expression, the role and function of its ABC transporters is unexplored. In this work, we investigated the Pichia ABC-B transporter STE6-2p. Functional investigations revealed that STE6-2p is capable of transporting rhodamines in vivo and is active in the presence of verapamil and triazoles in vitro. A phylogenetic analysis displays homology among multidrug resistance (MDR) transporters from pathogenic fungi to human ABC-B transporters. Further, we present high-resolution single-particle electron cryomicroscopy structures of an ABC transporter from P. pastoris in the apo conformation (3.1 A) and in complex with verapamil and adenylyl imidodiphosphate (AMP-PNP) (3.2 A). An unknown density between transmembrane helices 4, 5, and 6 in both structures suggests the presence of a sterol-binding site of unknown function.

Structural and functional investigation of ABC transporter STE6-2p from Pichia pastoris reveals unexpected interaction with sterol molecules.,Schleker ESM, Buschmann S, Xie H, Welsch S, Michel H, Reinhart C Proc Natl Acad Sci U S A. 2022 Oct 25;119(43):e2202822119. doi: , 10.1073/pnas.2202822119. Epub 2022 Oct 18. PMID:36256814<ref>PMID:36256814</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7qkr" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Komagataella phaffii CBS 7435]]
[[Category: Large Structures]]
[[Category: Reinhart C]]
[[Category: Schleker ESM]]