View source for 8vp3


==Cryo-EM structure of the ABC transporter PCAT1 bound with MgADP and Substrate==
<StructureSection load='8vp3' size='340' side='right'caption='[[8vp3]], [[Resolution|resolution]] 2.96&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8vp3]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Acetivibrio_thermocellus_ATCC_27405 Acetivibrio thermocellus ATCC 27405]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8VP3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8VP3 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]] 2.96&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=A1ACX:(4S)-4-hydroxy-N,N,N-trimethyl-4,10-dioxo-3,5,9-trioxa-4lambda~5~-phosphapentacosan-1-aminium'>A1ACX</scene>, <scene name='pdbligand=ADP:ADENOSINE-5-DIPHOSPHATE'>ADP</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=POV:(2S)-3-(HEXADECANOYLOXY)-2-[(9Z)-OCTADEC-9-ENOYLOXY]PROPYL+2-(TRIMETHYLAMMONIO)ETHYL+PHOSPHATE'>POV</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=8vp3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8vp3 OCA], [https://pdbe.org/8vp3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8vp3 RCSB], [https://www.ebi.ac.uk/pdbsum/8vp3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8vp3 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A3DCU1_ACET2 A3DCU1_ACET2] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Protease-containing ABC transporters (PCATs) couple the energy of ATP hydrolysis to the processing and export of diverse cargo proteins across cell membranes to mediate antimicrobial resistance and quorum sensing. Here, we combine biochemical analysis, single particle cryoEM, and DEER spectroscopy in lipid bilayers along with computational analysis to illuminate the structural and energetic underpinnings of coupled cargo protein export. Our integrated investigation uncovers competitive interplay between nucleotides and cargo protein binding that ensures the latter's orderly processing and subsequent transport. The energetics of cryoEM structures in lipid bilayers are congruent with the inferred mechanism from ATP turnover analysis and reveal a snapshot of a high-energy outward-facing conformation that provides an exit pathway into the lipid bilayer and/or the extracellular side. DEER investigation of the core ABC transporter suggests evolutionary tuning of the energetic landscape to fulfill the function of substrate processing prior to export.

Conformational cycle of a protease-containing ABC transporter in lipid nanodiscs reveals the mechanism of cargo-protein coupling.,Zhang R, Jagessar KL, Brownd M, Polasa A, Stein RA, Moradi M, Karakas E, Mchaourab HS Nat Commun. 2024 Oct 20;15(1):9055. doi: 10.1038/s41467-024-53420-0. PMID:39428489<ref>PMID:39428489</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8vp3" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Acetivibrio thermocellus ATCC 27405]]
[[Category: Large Structures]]
[[Category: Brownd M]]
[[Category: Jagessar KL]]
[[Category: Karakas E]]
[[Category: Mchaourab HS]]
[[Category: Moradi M]]
[[Category: Polasa A]]
[[Category: Stein R]]
[[Category: Zhang R]]