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| | ==Asymmetric structure of trimeric AcrB from Escherichia coli== | | ==Asymmetric structure of trimeric AcrB from Escherichia coli== |
| - | <StructureSection load='2hrt' size='340' side='right' caption='[[2hrt]], [[Resolution|resolution]] 3.00Å' scene=''> | + | <StructureSection load='2hrt' size='340' side='right'caption='[[2hrt]], [[Resolution|resolution]] 3.00Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2hrt]] is a 6 chain structure with sequence from [http://en.wikipedia.org/wiki/Ecoli Ecoli]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2HRT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2hrt]] is a 6 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HRT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2HRT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 3Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">acrB, acrE ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=83333 ECOLI])</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=FLC:CITRATE+ANION'>FLC</scene></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2hrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hrt OCA], [http://pdbe.org/2hrt PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2hrt RCSB], [http://www.ebi.ac.uk/pdbsum/2hrt PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2hrt 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=2hrt FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2hrt OCA], [https://pdbe.org/2hrt PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2hrt RCSB], [https://www.ebi.ac.uk/pdbsum/2hrt PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2hrt ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI]] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref> | + | [https://www.uniprot.org/uniprot/ACRB_ECOLI ACRB_ECOLI] AcrAB is a drug efflux protein with a broad substrate specificity.<ref>PMID:16915237</ref> <ref>PMID:16946072</ref> <ref>PMID:17194213</ref> |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Ecoli]] | + | [[Category: Escherichia coli K-12]] |
| - | [[Category: Diederichs, K]] | + | [[Category: Large Structures]] |
| - | [[Category: Eicher, T]] | + | [[Category: Diederichs K]] |
| - | [[Category: Pos, K M]] | + | [[Category: Eicher T]] |
| - | [[Category: Schiefner, A]] | + | [[Category: Pos KM]] |
| - | [[Category: Seeger, M A]] | + | [[Category: Schiefner A]] |
| - | [[Category: Verrey, F]] | + | [[Category: Seeger MA]] |
| - | [[Category: Acra]]
| + | [[Category: Verrey F]] |
| - | [[Category: Acrb]]
| + | |
| - | [[Category: Antibiotic resistance]]
| + | |
| - | [[Category: Membrane protein]]
| + | |
| - | [[Category: Multidrug efflux pump]]
| + | |
| - | [[Category: Proton-coupled exchanger]]
| + | |
| - | [[Category: Rnd]]
| + | |
| - | [[Category: Tolc]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3]
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
The AcrA/AcrB/TolC complex spans the inner and outer membranes of Escherichia coli and serves as its major drug-resistance pump. Driven by the proton motive force, it mediates the efflux of bile salts, detergents, organic solvents, and many structurally unrelated antibiotics. Here, we report a crystallographic structure of trimeric AcrB determined at 2.9 and 3.0 angstrom resolution in space groups that allow asymmetry of the monomers. This structure reveals three different monomer conformations representing consecutive states in a transport cycle. The structural data imply an alternating access mechanism and a novel peristaltic mode of drug transport by this type of transporter.
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism.,Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072[4]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Murakami S, Nakashima R, Yamashita E, Matsumoto T, Yamaguchi A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism. Nature. 2006 Sep 14;443(7108):173-9. Epub 2006 Aug 16. PMID:16915237 doi:10.1038/nature05076
- ↑ Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295
- ↑ Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors. PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213 doi:10.1371/journal.pbio.0050007
- ↑ Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM. Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism. Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072 doi:313/5791/1295
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