2btn
From Proteopedia
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|PDB= 2btn |SIZE=350|CAPTION= <scene name='initialview01'>2btn</scene>, resolution 2.00Å | |PDB= 2btn |SIZE=350|CAPTION= <scene name='initialview01'>2btn</scene>, resolution 2.00Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+A'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2btn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2btn OCA], [http://www.ebi.ac.uk/pdbsum/2btn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2btn RCSB]</span> | ||
}} | }} | ||
| Line 32: | Line 35: | ||
[[Category: Lee, J S.]] | [[Category: Lee, J S.]] | ||
[[Category: Oh, T K.]] | [[Category: Oh, T K.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: ZN]] | ||
[[Category: n-acyl homoserine lactone hydrolase]] | [[Category: n-acyl homoserine lactone hydrolase]] | ||
[[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 Mon Mar 31 02:11:38 2008'' |
Revision as of 23:11, 30 March 2008
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| , resolution 2.00Å | |||||||
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| Ligands: | , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
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