2btn
From Proteopedia
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==Overview== | ==Overview== | ||
- | In many Gram-negative bacteria, including a number of pathogens such as | + | 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. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Bacillus thuringiensis]] | [[Category: Bacillus thuringiensis]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
- | [[Category: Choi, W | + | [[Category: Choi, W C.]] |
- | [[Category: Derewenda, Z | + | [[Category: Derewenda, Z S.]] |
- | [[Category: Kang, B | + | [[Category: Kang, B S.]] |
- | [[Category: Kang, H | + | [[Category: Kang, H O.]] |
- | [[Category: Kim, K | + | [[Category: Kim, K J.]] |
- | [[Category: Kim, M | + | [[Category: Kim, M H.]] |
- | [[Category: Lee, C | + | [[Category: Lee, C H.]] |
- | [[Category: Lee, J | + | [[Category: Lee, J K.]] |
- | [[Category: Lee, J | + | [[Category: Lee, J S.]] |
- | [[Category: Oh, T | + | [[Category: Oh, T K.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: quorum sensing]] | [[Category: quorum sensing]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:41:30 2008'' |
Revision as of 14:41, 21 February 2008
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CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF THE QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE HYDROLASE
Overview
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.
About this Structure
2BTN is a Single protein structure of sequence from Bacillus thuringiensis with and as ligands. Known structural/functional Site: . Full crystallographic information is available from OCA.
Reference
The molecular structure and catalytic mechanism of a quorum-quenching N-acyl-L-homoserine lactone hydrolase., Kim MH, Choi WC, Kang HO, Lee JS, Kang BS, Kim KJ, Derewenda ZS, Oh TK, Lee CH, Lee JK, Proc Natl Acad Sci U S A. 2005 Dec 6;102(49):17606-11. Epub 2005 Nov 28. PMID:16314577
Page seeded by OCA on Thu Feb 21 16:41:30 2008