2a7m
From Proteopedia
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1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis
Overview
The three-dimensional structure of the N-acyl-l-homoserine lactone, hydrolase (AHL lactonase) from Bacillus thuringiensis has been determined, by using single-wavelength anomalous dispersion (SAD) phasing, to, 1.6-angstroms resolution. AHLs are produced by many Gram-negative bacteria, as signaling molecules used in quorum-sensing pathways that indirectly, sense cell density and regulate communal behavior. Because of their, importance in pathogenicity, quorum-sensing pathways have been suggested, as potential targets for the development of novel therapeutics., Quorum-sensing can be disrupted by enzymes evolved to degrade these, lactones, such as AHL lactonases. These enzymes are members of the, metallo-beta-lactamase superfamily and contain two zinc ions in their, active sites. The zinc ions are coordinated to a number of ligands, including a single oxygen of a bridging carboxylate and a bridging, water/hydroxide ion, thought to be the nucleophile that hydrolyzes the, AHLs to ring-opened products, which can no longer act as quorum signals.
About this Structure
2A7M is a Single protein structure of sequence from Bacillus thuringiensis serovar kurstaki with and as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis., Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D, Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11882-7. Epub 2005 Aug 8. PMID:16087890
Page seeded by OCA on Tue Jan 29 17:56:13 2008
