6CGZ

Structure of the Quorum Quenching lactonase from Alicyclobacillus acidoterrestris bound to C6-AHL

6CGZ の概要

• エントリーDOI: 10.2210/pdb6cgz/pdb
• 関連するPDBエントリー: 6CGY
• 分子名称: Beta-lactamase, COBALT (II) ION, 1,2-ETHANEDIOL, ... (7 entities in total)
• 機能のキーワード: lactonase, acyl homoserine lactone hydrolase, hydrolase
• 由来する生物種: Alicyclobacillus acidoterrestris (strain ATCC 49025 / DSM 3922 / CIP 106132 / NCIMB 13137 / GD3B)
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 98457.81

構造登録者

Bergonzi, C.,Schwab, M.,Naik, T.,Daude, D.,Chabriere, E.,Elias, M. (登録日: 2018-02-21, 公開日: 2018-08-15, 最終更新日: 2024-03-13)

主引用文献

Bergonzi, C.,Schwab, M.,Naik, T.,Daude, D.,Chabriere, E.,Elias, M.
Structural and Biochemical Characterization of AaL, a Quorum Quenching Lactonase with Unusual Kinetic Properties.
Sci Rep, 8:11262-11262, 2018

PubMed Abstract: Quorum quenching lactonases are enzymes that are capable of disrupting bacterial signaling based on acyl homoserine lactones (AHL) via their enzymatic degradation. In particular, lactonases have therefore been demonstrated to inhibit bacterial behaviors that depend on these chemicals, such as the formation of biofilms or the expression of virulence factors. Here we characterized biochemically and structurally a novel representative from the metallo-β-lactamase superfamily, named AaL that was isolated from the thermoacidophilic bacterium Alicyclobacillus acidoterrestris. AaL is a potent quorum quenching enzyme as demonstrated by its ability to inhibit the biofilm formation of Acinetobacter baumannii. Kinetic studies demonstrate that AaL is both a proficient and a broad spectrum enzyme, being capable of hydrolyzing a wide range of lactones with high rates (k/K > 10 M.s). Additionally, AaL exhibits unusually low K values, ranging from 10 to 80 µM. Analysis of AaL structures bound to phosphate, glycerol, and C6-AHL reveals a unique hydrophobic patch (W26, F87 and I237), involved in substrate binding, possibly accounting for the enzyme's high specificity. Identifying the specificity determinants will aid the development of highly specific quorum quenching enzymes as potential therapeutics.

PubMed: 30050039
DOI: 10.1038/s41598-018-28988-5

実験手法

X-RAY DIFFRACTION (1.8 Å)