1OY8: Structural Basis Of Multiple Drug Binding Capacity Of The Acrb Multidrug Efflux Pump

Citation:
Abstract
Multidrug efflux pumps cause serious problems in cancer chemotherapy and treatment of bacterial infections. Yet high-resolution structures of ligand transporter complexes have previously been unavailable. We obtained x-ray crystallographic structures of the trimeric AcrB pump from Escherichia coli with four structurally diverse ligands. The structures show that three molecules of ligands bind simultaneously to the extremely large central cavity of 5000 cubic angstroms, primarily by hydrophobic, aromatic stacking and van der Waals interactions. Each ligand uses a slightly different subset of AcrB residues for binding. The bound ligand molecules often interact with each other, stabilizing the binding.
PDB ID: 1OY8Download
MMDB ID: 23129
PDB Deposition Date: 2003/4/3
Updated in MMDB: 2007/10
Experimental Method:
x-ray diffraction
Resolution: 3.63  Å
Source Organism:
Similar Structures:
Biological Unit for 1OY8: trimeric; determined by author and by software (PISA,PQS)
Molecular Components in 1OY8
Label Count Molecule
Proteins (3 molecules)
3
Acriflavine Resistance Protein B(Gene symbol: acrB)
Molecule annotation
Chemicals (3 molecules)
1
3
* Click molecule labels to explore molecular sequence information.

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