2BTN

Crystal Structure and Catalytic Mechanism of the Quorum-Quenching N- Acyl Homoserine Lactone Hydrolase

Summary for 2BTN

• Entry DOI: 10.2210/pdb2btn/pdb
• Related: 2A7M 2BR6
• Descriptor: AIIA-LIKE PROTEIN, ZINC ION, GLYCEROL, ... (4 entities in total)
• Functional Keywords: hydrolase, n-acyl homoserine lactone hydrolase, quorum sensing
• Biological source: BACILLUS THURINGIENSIS
• Total number of polymer chains: 1
• Total formula weight: 28811.52

Authors

Kim, M.H.,Choi, W.C.,Kang, H.O.,Lee, J.S.,Kang, B.S.,Kim, K.J.,Derewenda, Z.S.,Oh, T.K.,Lee, C.H.,Lee, J.K. (deposition date: 2005-06-03, release date: 2005-12-07, Last modification date: 2024-05-08)

Primary citation

Kim, M.H.,Choi, W.C.,Kang, H.O.,Lee, J.S.,Kang, B.S.,Kim, K.J.,Derewenda, Z.S.,Oh, T.K.,Lee, C.H.,Lee, J.K.
The Molecular Structure and Catalytic Mechanism of a Quorum-Quenching N-Acyl-L-Homoserine Lactone Hydrolase.
Proc.Natl.Acad.Sci.USA, 102:17606-, 2005

PubMed 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-angstroms resolution structure of the AHL-lactonase from Bacillus thuringiensis and a 1.7-angstroms 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-beta-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.

PubMed: 16314577
DOI: 10.1073/PNAS.0504996102

Experimental method

X-RAY DIFFRACTION (2 Å)