View source for 8ufe


==Multidrug efflux pump EfpA from mycobacterium smegmatis==
<StructureSection load='8ufe' size='340' side='right'caption='[[8ufe]], [[Resolution|resolution]] 3.68&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8ufe]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mycolicibacterium_smegmatis Mycolicibacterium smegmatis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=8UFE OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8UFE 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]] 3.68&#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=8ufe FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8ufe OCA], [https://pdbe.org/8ufe PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8ufe RCSB], [https://www.ebi.ac.uk/pdbsum/8ufe PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8ufe ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/A0A653FLF0_MYCSM A0A653FLF0_MYCSM] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
As the first identified multidrug efflux pump in Mycobacterium tuberculosis (Mtb), EfpA is an essential protein and promising drug target. However, the functional and inhibitory mechanisms of EfpA are poorly understood. Here we report cryo-EM structures of EfpA in outward-open conformation, either bound to three endogenous lipids or the inhibitor BRD-8000.3. Three lipids inside EfpA span from the inner leaflet to the outer leaflet of the membrane. BRD-8000.3 occupies one lipid site at the level of inner membrane leaflet, competitively inhibiting lipid binding. EfpA resembles the related lysophospholipid transporter MFSD2A in both overall structure and lipid binding sites and may function as a lipid flippase. Combining AlphaFold-predicted EfpA structure, which is inward-open, we propose a complete conformational transition cycle for EfpA. Together, our results provide a structural and mechanistic foundation to comprehend EfpA function and develop EfpA-targeting anti-TB drugs.

Structures of the Mycobacterium tuberculosis efflux pump EfpA reveal the mechanisms of transport and inhibition.,Wang S, Wang K, Song K, Lai ZW, Li P, Li D, Sun Y, Mei Y, Xu C, Liao M Nat Commun. 2024 Sep 4;15(1):7710. doi: 10.1038/s41467-024-51948-9. PMID:39231991<ref>PMID:39231991</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8ufe" style="background-color:#fffaf0;"></div>
== References ==
<references/>
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</StructureSection>
[[Category: Large Structures]]
[[Category: Mycolicibacterium smegmatis]]
[[Category: Liao M]]
[[Category: Wang S]]