Abstract:
: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.
journal_name
Proc Natl Acad Sci U S Aauthors
Liu D,Lepore BW,Petsko GA,Thomas PW,Stone EM,Fast W,Ringe Ddoi
10.1073/pnas.0505255102keywords:
subject
Has Abstractpub_date
2005-08-16 00:00:00pages
11882-7issue
33eissn
0027-8424issn
1091-6490pii
0505255102journal_volume
102pub_type
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