2BR6
Crystal Structure of Quorum-Quenching N-Acyl Homoserine Lactone Lactonase
Summary for 2BR6
| Entry DOI | 10.2210/pdb2br6/pdb |
| Related | 2A7M 2BTN |
| Descriptor | AIIA-LIKE PROTEIN, ZINC ION, GLYCEROL, ... (5 entities in total) |
| Functional Keywords | quorum sensing, quorum-quenching enzyme, acyl-hsl lactonase, acyl-homoserine, hydrolase |
| Biological source | BACILLUS THURINGIENSIS |
| Total number of polymer chains | 1 |
| Total formula weight | 28912.62 |
| Authors | Kim, M.H.,Choi, W.C.,Kang, H.O.,Kang, B.S.,Kim, K.J.,Derewenda, Z.S.,Lee, J.K.,Oh, T.K.,Lee, C.H. (deposition date: 2005-05-03, 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 Cited by 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: 16314577DOI: 10.1073/PNAS.0504996102 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.7 Å) |
Structure validation
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