2br6
From Proteopedia
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| - | [[Image:2br6.gif|left|200px]]<br /><applet load="2br6" size=" | + | [[Image:2br6.gif|left|200px]]<br /><applet load="2br6" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="2br6, resolution 1.70Å" /> | caption="2br6, resolution 1.70Å" /> | ||
'''CRYSTAL STRUCTURE OF QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE LACTONASE'''<br /> | '''CRYSTAL STRUCTURE OF QUORUM-QUENCHING N-ACYL HOMOSERINE LACTONE LACTONASE'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 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 ZN, HSL and GOL 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:// | + | 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]. |
==Reference== | ==Reference== | ||
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[[Category: quorum-quenching enzyme]] | [[Category: quorum-quenching enzyme]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Feb 3 10:26:57 2008'' |
Revision as of 08:26, 3 February 2008
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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 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 Sun Feb 3 10:26:57 2008
Categories: Bacillus thuringiensis | Single protein | Choi, W.C. | Derewenda, Z.S. | Kang, B.S. | Kang, H.O. | Kim, K.J. | Kim, M.H. | Lee, C.H. | Lee, J.K. | Oh, T.K. | GOL | HSL | ZN | Acyl-homoserine | Acyl-hsl lactonase | Hydrolase | Quorum sensing | Quorum-quenching enzyme
