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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.

Author information

1
Biochemistry, Molecular Biology and Biophysics Department and BioTechnology Institute, University of Minnesota, Saint Paul, MN 55108, USA.
2
URMITE, Aix Marseille Université, INSERM, CNRS, IRD, 27 Boulevard Jean Moulin, 13385 Marseille, France.

Abstract

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.

KEYWORDS:

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

PMID:
28777091
PMCID:
PMC5544005
DOI:
10.1107/S2053230X17010640
[Indexed for MEDLINE]
Free PMC Article

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