2DHH
Crystal structure of a multidrug transporter reveal a functionally rotating mechanism
Summary for 2DHH
| Entry DOI | 10.2210/pdb2dhh/pdb |
| Related | 2DR6 2DRD |
| Descriptor | ACRB (2 entities in total) |
| Functional Keywords | membrane transporter, membrane protein, multidrug efflux, drug resistance, transporter, exporter, antiporter |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane; Multi-pass membrane protein: P31224 |
| Total number of polymer chains | 3 |
| Total formula weight | 342653.23 |
| Authors | Murakami, S.,Nakashima, R.,Yamashita, E.,Matsumoto, T. (deposition date: 2006-03-23, release date: 2006-08-22, Last modification date: 2024-03-13) |
| Primary citation | Murakami, S.,Nakashima, R.,Yamashita, E.,Matsumoto, T.,Yamaguchi, A. Crystal structures of a multidrug transporter reveal a functionally rotating mechanism Nature, 443:173-179, 2006 Cited by PubMed 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. PubMed: 16915237DOI: 10.1038/nature05076 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
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