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Acta Crystallogr F Struct Biol Commun. 2017 Aug 1;73(Pt 8):476-480. doi: 10.1107/S2053230X17010640. Epub 2017 Jul 26.

The quorum-quenching lactonase from Alicyclobacter acidoterrestris: purification, kinetic characterization, crystallization and crystallographic analysis.

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Biochemistry, Molecular Biology and Biophysics Department and BioTechnology Institute, University of Minnesota, Saint Paul, MN 55108, USA.
URMITE, Aix Marseille Université, INSERM, CNRS, IRD, 27 Boulevard Jean Moulin, 13385 Marseille, France.


Lactonases comprise a class of enzymes that hydrolyze lactones, including acyl-homoserine lactones (AHLs); the latter are used as chemical signaling molecules by numerous Gram-negative bacteria. Lactonases have therefore been demonstrated to quench AHL-based bacterial communication. In particular, lactonases are capable of inhibiting bacterial behaviors that depend on these chemicals, such as the formation of biofilms or the expression of virulence factors. A novel representative from the metallo-β-lactamase superfamily, named AaL, was isolated from the thermoacidophilic bacterium Alicyclobacter acidoterrestris. Kinetic characterization proves AaL to be a proficient lactonase, with catalytic efficiencies (kcat/Km) against AHLs in the region of 105 M-1 s-1. AaL exhibits a very broad substrate specificity. Its structure is expected to reveal the molecular determinants for its substrate binding and specificity, as well as to provide grounds for future protein-engineering projects. Here, the expression, purification, characterization, crystallization and X-ray diffraction data collection of AaL at 1.65 Å resolution are reported.


Alicyclobacter acidoterrestris; lactonases; quorum quenching; quorum sensing; thermophiles

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