2A7M

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

Summary for 2A7M

• Entry DOI: 10.2210/pdb2a7m/pdb
• Descriptor: N-acyl homoserine lactone hydrolase, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: bimetallohydrolase, hydrolase, bimetallo di-zinc, lactonase acyl homoserine, quorum quenching n-acyl, n-acyl
• Biological source: Bacillus thuringiensis serovar kurstaki
• Total number of polymer chains: 1
• Total formula weight: 29117.73

Authors

Liu, D.,Lepore, B.W.,Petsko, G.A.,Thomas, P.W.,Stone, E.M.,Fast, W.,Ringe, D. (deposition date: 2005-07-05, release date: 2005-08-16, Last modification date: 2024-02-14)

Primary citation

Liu, D.,Lepore, B.W.,Petsko, G.A.,Thomas, P.W.,Stone, E.M.,Fast, W.,Ringe, D.
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis
Proc.Natl.Acad.Sci.Usa, 102:11882-11887, 2005

PubMed 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.

PubMed: 16087890
DOI: 10.1073/pnas.0505255102

Experimental method

X-RAY DIFFRACTION (1.6 Å)