2HRT

Asymmetric structure of trimeric AcrB from Escherichia coli

Summary for 2HRT

• Entry DOI: 10.2210/pdb2hrt/pdb
• Descriptor: Acriflavine resistance protein B, CITRATE ANION (2 entities in total)
• Functional Keywords: acrb, multidrug efflux pump, rnd, antibiotic resistance, acra, tolc, membrane protein, proton-coupled exchanger, transport protein
• Biological source: Escherichia coli K12
• Cellular location: Cell inner membrane; Multi-pass membrane protein: P31224
• Total number of polymer chains: 6
• Total formula weight: 689174.13

Authors

Seeger, M.A.,Schiefner, A.,Eicher, T.,Verrey, F.,Diederichs, K.,Pos, K.M. (deposition date: 2006-07-20, 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

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: 16946072
DOI: 10.1126/science.1131542

Experimental method

X-RAY DIFFRACTION (3 Å)