2a7m
From Proteopedia
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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''' | ||
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[[Category: Stone, E M.]] | [[Category: Stone, E M.]] | ||
[[Category: Thomas, P W.]] | [[Category: Thomas, P W.]] | ||
- | [[Category: | + | [[Category: Bimetallo di-zinc]] |
- | [[Category: | + | [[Category: Bimetallohydrolase]] |
- | [[Category: | + | [[Category: Hydrolase]] |
- | [[Category: | + | [[Category: Lactonase acyl homoserine]] |
- | [[Category: | + | [[Category: N-acyl]] |
- | [[Category: | + | [[Category: Quorum quenching n-acyl]] |
- | [[Category: | + | [[Category: Zinc]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 18:42:36 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 15:42, 3 May 2008
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. 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 Sat May 3 18:42:36 2008