The quorum‐quenching lactonase from Alicyclobacter acidoterrestris: purification, kinetic characterization, crystallization and crystallographic analysis. Issue 8 (1st August 2017)

• Record Type: Journal Article
• Authors: Bergonzi, Celine; Schwab, Michael; Chabriere, Eric; Elias, Mikael
• Is Part Of: Acta crystallographica. Volume 73:Issue 8(2017:Aug.)
• Page Start: 476
• Page End: 480
• Publication Date: 2017-08-01
• Subjects: quorum sensing -- quorum quenching -- lactonases -- thermophiles -- Alicyclobacter acidoterrestris; Crystallography -- Periodicals; Crystals -- Periodicals; 548
• DOI: 10.1107/S2053230X17010640
• Languages: English
• ISSNs: 2053-230X

Abstract

Abstract : A lactonase from Alicyclobacter acidoterrestris named AaL has been isolated, purified, characterized and crystallized. The structure of AaL is expected to provide insights regarding its catalytic mechanism of lactone hydrolysis. 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 ( k cat / K m ) against AHLs in the region of 10 5 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.