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(New page: 200px<br /> <applet load="2btn" size="450" color="white" frame="true" align="right" spinBox="true" caption="2btn, resolution 2.00Å" /> '''CRYSTAL STRUCTURE A...)
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Revision as of 19:52, 29 October 2007
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CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF THE QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE HYDROLASE
Overview
In many Gram-negative bacteria, including a number of pathogens such as, Pseudomonas aeruginosa and Erwinia carotovora, virulence factor production, and biofilm formation are linked to the quorum-sensing systems that use, diffusible N-acyl-L-homoserine lactones (AHLs) as intercellular messenger, molecules. A number of organisms also contain genes coding for lactonases, that hydrolyze AHLs into inactive products, thereby blocking the, quorum-sensing systems. Consequently, these enzymes attract intense, interest for the development of antiinfection therapies. However, the, catalytic mechanism of AHL-lactonase is poorly understood and subject to, controversy. We here report a 2.0-angstroms resolution structure of the, AHL-lactonase from Bacillus thuringiensis and a 1.7-angstroms crystal, ... [(full description)]
About this Structure
2BTN is a [Single protein] structure of sequence from [Bacillus thuringiensis] with ZN and GOL as [ligands]. Full crystallographic information is available from [OCA].
Reference
The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase., Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK, Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17606-11. Epub 2005 Nov 28. PMID:16314577
Page seeded by OCA on Mon Oct 29 21:56:56 2007
