2a7m: Difference between revisions

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{{STRUCTURE_2a7m|  PDB=2a7m  |  SCENE=  }}  
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'''1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis'''
===1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis===




==Overview==
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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.
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==About this Structure==
==About this Structure==
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[[Category: Quorum quenching n-acyl]]
[[Category: Quorum quenching n-acyl]]
[[Category: Zinc]]
[[Category: Zinc]]
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Revision as of 11:22, 29 July 2008

File:2a7m.png

Template:STRUCTURE 2a7m

1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis

Template:ABSTRACT PUBMED 16087890

About this Structure

2A7M is a Single protein structure of sequence from Bacillus thuringiensis serovar kurstaki. 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

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