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

The quorum‐quenching lactonase from Alicyclobacter acidoterrestris: purification, kinetic... 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. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Acta Crystallographica Section F Wiley

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

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Publisher
Wiley
Copyright
Copyright © 2017 Wiley Subscription Services
ISSN
2053-230X
eISSN
2053-230X
DOI
10.1107/S2053230X17010640
pmid
28777091
Publisher site
See Article on Publisher Site

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.

Journal

Acta Crystallographica Section F – Wiley

Published: Jan 1, 2017

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