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| | <SX load='6ows' size='340' side='right' viewer='molstar' caption='[[6ows]], [[Resolution|resolution]] 2.98Å' scene=''> | | <SX load='6ows' size='340' side='right' viewer='molstar' caption='[[6ows]], [[Resolution|resolution]] 2.98Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[6ows]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Aciba Aciba]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OWS OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=6OWS FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[6ows]] is a 3 chain structure with sequence from [https://en.wikipedia.org/wiki/Acinetobacter_baumannii Acinetobacter baumannii]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6OWS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=6OWS FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Electron Microscopy, [[Resolution|Resolution]] 2.98Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">adeB, acrB, 32_436, CBI29_01998, EA686_00900 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=470 ACIBA])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=PTY:PHOSPHATIDYLETHANOLAMINE'>PTY</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=6ows FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ows OCA], [http://pdbe.org/6ows PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=6ows RCSB], [http://www.ebi.ac.uk/pdbsum/6ows PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=6ows ProSAT]</span></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=6ows FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=6ows OCA], [https://pdbe.org/6ows PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=6ows RCSB], [https://www.ebi.ac.uk/pdbsum/6ows PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=6ows ProSAT]</span></td></tr> |
| | </table> | | </table> |
| - | <div style="background-color:#fffaf0;">
| + | == Function == |
| - | == Publication Abstract from PubMed == | + | [https://www.uniprot.org/uniprot/Q2FD70_ACIBA Q2FD70_ACIBA] |
| - | Resistance-nodulation-cell division multidrug efflux pumps are membrane proteins that catalyze the export of drugs and toxic compounds out of bacterial cells. Within the hydrophobe-amphiphile subfamily, these multidrug-resistant proteins form trimeric efflux pumps. The drug efflux process is energized by the influx of protons. Here, we use single-particle cryo-electron microscopy to elucidate the structure of the Acinetobacter baumannii AdeB multidrug efflux pump embedded in lipidic nanodiscs to a resolution of 2.98 A. We found that each AdeB molecule within the trimer preferentially takes the resting conformational state in the absence of substrates. We propose that proton influx and drug efflux are synchronized and coordinated within the transport cycle.IMPORTANCE Acinetobacter baumannii is a successful human pathogen which has emerged as one of the most problematic and highly antibiotic-resistant Gram-negative bacteria worldwide. Multidrug efflux is a major mechanism that A. baumannii uses to counteract the action of multiple classes of antibiotics, such as beta-lactams, tetracyclines, fluoroquinolones, and aminoglycosides. Here, we report a cryo-electron microscopy (cryo-EM) structure of the prevalent A. baumannii AdeB multidrug efflux pump, which indicates a plausible pathway for multidrug extrusion. Overall, our data suggest a mechanism for energy coupling that powers up this membrane protein to export antibiotics from bacterial cells. Our studies will ultimately inform an era in structure-guided drug design to combat multidrug resistance in these Gram-negative pathogens.
| + | |
| - | | + | |
| - | Cryo-Electron Microscopy Structure of an Acinetobacter baumannii Multidrug Efflux Pump.,Su CC, Morgan CE, Kambakam S, Rajavel M, Scott H, Huang W, Emerson CC, Taylor DJ, Stewart PL, Bonomo RA, Yu EW MBio. 2019 Jul 2;10(4). pii: mBio.01295-19. doi: 10.1128/mBio.01295-19. PMID:31266873<ref>PMID:31266873</ref>
| + | |
| - | | + | |
| - | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
| + | |
| - | </div>
| + | |
| - | <div class="pdbe-citations 6ows" style="background-color:#fffaf0;"></div>
| + | |
| - | == References ==
| + | |
| - | <references/>
| + | |
| | __TOC__ | | __TOC__ |
| | </SX> | | </SX> |
| - | [[Category: Aciba]] | + | [[Category: Acinetobacter baumannii]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Su, C C]] | + | [[Category: Su C-C]] |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Transporter]]
| + | |
