1t5e
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(New page: 200px<br /><applet load="1t5e" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t5e, resolution 3.Å" /> '''The structure of MexA'...)
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Revision as of 00:52, 21 November 2007
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The structure of MexA
Overview
Multidrug resistance among Gram-negative bacteria is conferred by, three-component membrane pumps that expel diverse antibiotics from the, cell. These efflux pumps consist of an inner membrane transporter such as, the AcrB proton antiporter, an outer membrane exit duct of the TolC, family, and a periplasmic protein known as the adaptor. We present the, x-ray structure of the MexA adaptor from the human pathogen Pseudomonas, aeruginosa. The elongated molecule contains three linearly arranged, subdomains; a 47-A-long alpha-helical hairpin, a lipoyl domain, and a, six-stranded beta-barrel. In the crystal, hairpins of neighboring MexA, monomers pack side-by-side to form twisted arcs. We discuss the, implications of the packing of molecules within the crystal. On the basis, of the structure and packing, we suggest a model for the key periplasmic, interaction between the outer membrane channel and the adaptor protein in, the assembled drug efflux pump.
About this Structure
1T5E is a Single protein structure of sequence from Pseudomonas aeruginosa with 3GR and GOL as ligands. Full crystallographic information is available from OCA.
Reference
Structure of the periplasmic component of a bacterial drug efflux pump., Higgins MK, Bokma E, Koronakis E, Hughes C, Koronakis V, Proc Natl Acad Sci U S A. 2004 Jul 6;101(27):9994-9. Epub 2004 Jun 28. PMID:15226509
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