Crystal structures of a multidrug transporter reveal a functionally rotating mechanism
AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which ha...
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| Published in | Nature Vol. 443; no. 7108; pp. 173 - 179 |
|---|---|
| Main Authors | , , , , |
| Format | Journal Article |
| Language | English |
| Published |
London
Nature Publishing
14.09.2006
Nature Publishing Group |
| Subjects | |
| Online Access | Get full text |
| ISSN | 0028-0836 1476-4687 1476-4687 1476-4679 |
| DOI | 10.1038/nature05076 |
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| Abstract | AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change. |
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| AbstractList | AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change. AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change. [PUBLICATION ABSTRACT] AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change.AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA. Here we describe crystal structures of AcrB with and without substrates. The AcrB-drug complex consists of three protomers, each of which has a different conformation corresponding to one of the three functional states of the transport cycle. Bound substrate was found in the periplasmic domain of one of the three protomers. The voluminous binding pocket is aromatic and allows multi-site binding. The structures indicate that drugs are exported by a three-step functionally rotating mechanism in which substrates undergo ordered binding change. |
| Audience | Academic |
| Author | Murakami, Satoshi Yamaguchi, Akihito Nakashima, Ryosuke Yamashita, Eiki Matsumoto, Takashi |
| Author_xml | – sequence: 1 givenname: Satoshi surname: Murakami fullname: Murakami, Satoshi – sequence: 2 givenname: Ryosuke surname: Nakashima fullname: Nakashima, Ryosuke – sequence: 3 givenname: Eiki surname: Yamashita fullname: Yamashita, Eiki – sequence: 4 givenname: Takashi surname: Matsumoto fullname: Matsumoto, Takashi – sequence: 5 givenname: Akihito surname: Yamaguchi fullname: Yamaguchi, Akihito |
| BackLink | http://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=18078525$$DView record in Pascal Francis https://www.ncbi.nlm.nih.gov/pubmed/16915237$$D View this record in MEDLINE/PubMed |
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| CODEN | NATUAS |
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| Snippet | AcrB is a principal multidrug efflux transporter in Escherichia coli that cooperates with an outer-membrane channel, TolC, and a membrane-fusion protein, AcrA.... |
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| SubjectTerms | Bacterial Outer Membrane Proteins - metabolism Binding Sites Biological and medical sciences Cell Membrane - metabolism Crystal structure Crystalline structure Crystallography, X-Ray E coli Escherichia coli Escherichia coli - chemistry Escherichia coli Proteins - chemistry Escherichia coli Proteins - metabolism Fundamental and applied biological sciences. Psychology Lipoproteins - metabolism Membrane Transport Proteins Membranes Minocycline - chemistry Minocycline - metabolism Models, Biological Models, Molecular Molecular biophysics Multidrug Resistance-Associated Proteins - chemistry Multidrug Resistance-Associated Proteins - metabolism Protein Structure, Secondary Protein Structure, Tertiary Proteins Rotation Structure in molecular biology Structure-Activity Relationship Substrate Specificity Substrates |
| Title | Crystal structures of a multidrug transporter reveal a functionally rotating mechanism |
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