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2br6

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[[Image:2br6.gif|left|200px]]<br /><applet load="2br6" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:2br6.gif|left|200px]]
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caption="2br6, resolution 1.70&Aring;" />
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'''CRYSTAL STRUCTURE OF QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE LACTONASE'''<br />
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{{Structure
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|PDB= 2br6 |SIZE=350|CAPTION= <scene name='initialview01'>2br6</scene>, resolution 1.70&Aring;
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|SITE= <scene name='pdbsite=AC1:Hsl+Binding+Site+For+Chain+A'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>, <scene name='pdbligand=HSL:HOMOSERINE+LACTONE'>HSL</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>
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|ACTIVITY=
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|GENE=
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}}
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'''CRYSTAL STRUCTURE OF QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE LACTONASE'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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2BR6 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 <scene name='pdbligand=ZN:'>ZN</scene>, <scene name='pdbligand=HSL:'>HSL</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Hsl+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BR6 OCA].
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2BR6 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Bacillus_thuringiensis Bacillus thuringiensis]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BR6 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=16314577 16314577]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/16314577 16314577]
[[Category: Bacillus thuringiensis]]
[[Category: Bacillus thuringiensis]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: quorum-quenching enzyme]]
[[Category: quorum-quenching enzyme]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:40:50 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:05:42 2008''

Revision as of 14:05, 20 March 2008

Image:2br6.gif


PDB ID 2br6

Drag the structure with the mouse to rotate
, resolution 1.70Å
Sites:
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE LACTONASE


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

2BR6 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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