2btn
From Proteopedia
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| - | [[Image:2btn.gif|left|200px]]<br /> | + | [[Image:2btn.gif|left|200px]]<br /><applet load="2btn" size="450" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="2btn" size="450" color="white" frame="true" align="right" spinBox="true" | + | |
caption="2btn, resolution 2.00Å" /> | caption="2btn, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF THE QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE HYDROLASE'''<br /> | '''CRYSTAL STRUCTURE AND CATALYTIC MECHANISM OF THE QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE HYDROLASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2BTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. | + | 2BTN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis] with ZN and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Gol Binding Site For Chain A'>AC1</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BTN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: quorum sensing]] | [[Category: quorum sensing]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Dec 18 18:58:09 2007'' |
Revision as of 16:48, 18 December 2007
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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 ZN and GOL 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
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