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| | <StructureSection load='4zit' size='340' side='right'caption='[[4zit]], [[Resolution|resolution]] 3.30Å' scene=''> | | <StructureSection load='4zit' size='340' side='right'caption='[[4zit]], [[Resolution|resolution]] 3.30Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4zit]] is a 6 chain structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4ZIT OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4ZIT FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4zit]] 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=4ZIT OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4ZIT FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</scene></td></tr> | + | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=LMT:DODECYL-BETA-D-MALTOSIDE'>LMT</scene>, <scene name='pdbligand=NI:NICKEL+(II)+ION'>NI</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=4zit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zit OCA], [http://pdbe.org/4zit PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4zit RCSB], [http://www.ebi.ac.uk/pdbsum/4zit PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4zit 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=4zit FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4zit OCA], [https://pdbe.org/4zit PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4zit RCSB], [https://www.ebi.ac.uk/pdbsum/4zit PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4zit 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> |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| | + | [[Category: Escherichia coli K-12]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Ababou, A]] | + | [[Category: Ababou A]] |
| - | [[Category: Koronakis, V]] | + | [[Category: Koronakis V]] |
| - | [[Category: Acrb]]
| + | |
| - | [[Category: Bacterial multidrug resistance]]
| + | |
| - | [[Category: Export mechanism]]
| + | |
| - | [[Category: Rnd efflux pump]]
| + | |
| - | [[Category: Transport protein]]
| + | |
| Structural highlights
Function
ACRB_ECOLI AcrAB is a drug efflux protein with a broad substrate specificity.[1] [2] [3]
Publication Abstract from PubMed
Gram-negative bacteria such as E. coli use tripartite efflux pumps such as AcrAB-TolC to expel antibiotics and noxious compounds. A key feature of the inner membrane transporter component, AcrB, is a short stretch of residues known as the gate/switch loop that divides the proximal and distal substrate binding pockets. Amino acid substitutions of the gate loop are known to decrease antibiotic resistance conferred by AcrB. Here we present two new AcrB gate loop variants, the first stripped of its bulky side chains, and a second in which the gate loop is removed entirely. By determining the crystal structures of the variant AcrB proteins in the presence and absence of erythromycin and assessing their ability to confer erythromycin tolerance, we demonstrate that the gate loop is important for AcrB export activity but is not required for erythromycin binding.
Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate.,Ababou A, Koronakis V PLoS One. 2016 Jul 12;11(7):e0159154. doi: 10.1371/journal.pone.0159154., eCollection 2016. PMID:27403665[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
- ↑ Ababou A, Koronakis V. Structures of Gate Loop Variants of the AcrB Drug Efflux Pump Bound by Erythromycin Substrate. PLoS One. 2016 Jul 12;11(7):e0159154. doi: 10.1371/journal.pone.0159154., eCollection 2016. PMID:27403665 doi:http://dx.doi.org/10.1371/journal.pone.0159154
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