2hrt
Asymmetric structure of trimeric AcrB from Escherichia coli
| |||||||
| , resolution 3.00Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | acrB, acrE (Escherichia coli) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
2HRT is a Single protein structure of sequence from Escherichia coli. Full crystallographic information is available from OCA.
ReferenceReference
Structural asymmetry of AcrB trimer suggests a peristaltic pump mechanism., Seeger MA, Schiefner A, Eicher T, Verrey F, Diederichs K, Pos KM, Science. 2006 Sep 1;313(5791):1295-8. PMID:16946072
Page seeded by OCA on Mon Mar 31 03:34:35 2008