2GIF
Asymmetric structure of trimeric AcrB from Escherichia coli
Summary for 2GIF
| Entry DOI | 10.2210/pdb2gif/pdb |
| Related | 1IWG |
| Descriptor | Acriflavine resistance protein B, CITRATE ANION (2 entities in total) |
| Functional Keywords | membrane protein, secondary transport, rnd, antibiotic resistance, drug-efflux pump, alternating site mechanism, membrane protein-transport protein complex, membrane protein/transport protein |
| Biological source | Escherichia coli |
| Cellular location | Cell inner membrane ; Multi- pass membrane protein : P31224 |
| Total number of polymer chains | 3 |
| Total formula weight | 344587.07 |
| Authors | Seeger, M.A.,Schiefner, A.,Eicher, T.,Verrey, F.,Diederichs, K.,Pos, K.M. (deposition date: 2006-03-28, release date: 2006-09-12, Last modification date: 2023-08-30) |
| Primary citation | Seeger, M.A.,Schiefner, A.,Eicher, T.,Verrey, F.,Diederichs, K.,Pos, K.M. Structural Asymmetry of AcrB Trimer Suggests a Peristaltic Pump Mechanism. Science, 313:1295-1298, 2006 Cited by PubMed Abstract: 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. PubMed: 16946072DOI: 10.1126/science.1131542 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.9 Å) |
Structure validation
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