1oye
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(New page: 200px<br /><applet load="1oye" size="450" color="white" frame="true" align="right" spinBox="true" caption="1oye, resolution 3.48Å" /> '''Structural Basis of ...)
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Revision as of 21:10, 20 November 2007
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Structural Basis of Multiple Binding Capacity of the AcrB multidrug Efflux Pump
Overview
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.
About this Structure
1OYE is a Single protein structure of sequence from Escherichia coli with CPF as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis of multiple drug-binding capacity of the AcrB multidrug efflux pump., Yu EW, McDermott G, Zgurskaya HI, Nikaido H, Koshland DE Jr, Science. 2003 May 9;300(5621):976-80. PMID:12738864
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