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Title 

The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase

Authors 

Myung Hee KimWon Chan ChoiHye Ok KangJong Suk LeeB S KangK J KimZ S DerewendaTae Kwang OhChoong Hwan LeeJung-Kee Lee

Publisher 

National Academy of Sciences

Issue Date 

2005

Citation 

Proceedings of the National Academy of Sciences of the United States of America, vol. 102, no. 49, pp. 17606-17611

Keywords 

crystal structurelactonasemetalloenzymequorum sensingglyoxalasehydrolasehydroxyacylglutathione hydrolasen acyl homoserine lactone hydrolaseribonucleaseribonuclease Z

Abstract 

In many Gram-negative bacteria, including a number of pathogens such as Pseudomonas aeruginosa and Erwinia carotovora, virulence factor production and biofilm formation are linked to the quorum-sensing systems that use diffusible N-acyl-L-homoserine lactones (AHLs) as intercellular messenger molecules. A number of organisms also contain genes coding for lactonases that hydrolyze AHLs into inactive products, thereby blocking the quorum-sensing systems. Consequently, these enzymes attract intense interest for the development of antiinfection therapies. However, the catalytic mechanism of AHL-lactonase is poorly understood and subject to controversy. We here report a 2.0-? resolution structure of the AHL-lactonase from Bacillus thuringiensis and a 1.7-? crystal structure of its complex with L-homoserine lactone. Despite limited sequence similarity, the enzyme shows remarkable structural similarities to glyoxalase II and RNase Z proteins, members of the metallo-β-lactamase superfamily. We present experimental evidence that AHL-lactonase is a metalloenzyme containing two zinc ions involved in catalysis, and we propose a catalytic mechanism for bacterial metallo-AHL-lactonases.

ISSN 

0027-8424

Link 

http://dx.doi.org/10.1073/pnas.0504996102

Appears in Collections

1. Journal Articles > Journal Articles

Registered Date

2017-04-19


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