2j8s: Difference between revisions
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<StructureSection load='2j8s' size='340' side='right'caption='[[2j8s]], [[Resolution|resolution]] 2.54Å' scene=''> | <StructureSection load='2j8s' size='340' side='right'caption='[[2j8s]], [[Resolution|resolution]] 2.54Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[2j8s]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[2j8s]] is a 5 chain structure with sequence from [https://en.wikipedia.org/wiki/Escherichia_coli_K-12 Escherichia coli K-12] and [https://en.wikipedia.org/wiki/Synthetic_construct Synthetic construct]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2J8S OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2J8S FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.54Å</td></tr> | ||
<tr id=' | <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=LMU:DODECYL-ALPHA-D-MALTOSIDE'>LMU</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=2j8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8s OCA], [https://pdbe.org/2j8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8s RCSB], [https://www.ebi.ac.uk/pdbsum/2j8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8s 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=2j8s FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2j8s OCA], [https://pdbe.org/2j8s PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2j8s RCSB], [https://www.ebi.ac.uk/pdbsum/2j8s PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2j8s ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[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: | [[Category: Escherichia coli K-12]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Synthetic construct | [[Category: Synthetic construct]] | ||
[[Category: Amstutz | [[Category: Amstutz P]] | ||
[[Category: Briand | [[Category: Briand C]] | ||
[[Category: Gruetter | [[Category: Gruetter MG]] | ||
[[Category: Sennhauser | [[Category: Sennhauser G]] | ||
[[Category: Storchenegger | [[Category: Storchenegger O]] | ||
Latest revision as of 17:38, 13 December 2023
Drug Export Pathway of Multidrug Exporter AcrB Revealed by DARPin InhibitorsDrug Export Pathway of Multidrug Exporter AcrB Revealed by DARPin Inhibitors
Structural highlights
FunctionACRB_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 PubMedThe multidrug exporter AcrB is the inner membrane component of the AcrAB-TolC drug efflux system in Escherichia coli and is responsible for the resistance of this organism to a wide range of drugs. Here we describe the crystal structure of the trimeric AcrB in complex with a designed ankyrin-repeat protein (DARPin) inhibitor at 2.5-A resolution. The three subunits of AcrB are locked in different conformations revealing distinct channels in each subunit. There seems to be remote conformational coupling between the channel access, exit, and the putative proton-translocation site, explaining how the proton motive force is used for drug export. Thus our structure suggests a transport pathway not through the central pore but through the identified channels in the individual subunits, which greatly advances our understanding of the multidrug export mechanism. Drug export pathway of multidrug exporter AcrB revealed by DARPin inhibitors.,Sennhauser G, Amstutz P, Briand C, Storchenegger O, Grutter MG PLoS Biol. 2007 Jan;5(1):e7. PMID:17194213[4] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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