2a7m
From Proteopedia
(New page: 200px<br /><applet load="2a7m" size="350" color="white" frame="true" align="right" spinBox="true" caption="2a7m, resolution 1.60Å" /> '''1.6 Angstrom Resolut...) |
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==Overview== | ==Overview== | ||
| - | The three-dimensional structure of the N-acyl-l-homoserine lactone | + | The three-dimensional structure of the N-acyl-l-homoserine lactone hydrolase (AHL lactonase) from Bacillus thuringiensis has been determined, by using single-wavelength anomalous dispersion (SAD) phasing, to 1.6-angstroms resolution. AHLs are produced by many Gram-negative bacteria as signaling molecules used in quorum-sensing pathways that indirectly sense cell density and regulate communal behavior. Because of their importance in pathogenicity, quorum-sensing pathways have been suggested as potential targets for the development of novel therapeutics. Quorum-sensing can be disrupted by enzymes evolved to degrade these lactones, such as AHL lactonases. These enzymes are members of the metallo-beta-lactamase superfamily and contain two zinc ions in their active sites. The zinc ions are coordinated to a number of ligands, including a single oxygen of a bridging carboxylate and a bridging water/hydroxide ion, thought to be the nucleophile that hydrolyzes the AHLs to ring-opened products, which can no longer act as quorum signals. |
==About this Structure== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Fast, W.]] | [[Category: Fast, W.]] | ||
| - | [[Category: Lepore, B | + | [[Category: Lepore, B W.]] |
[[Category: Liu, D.]] | [[Category: Liu, D.]] | ||
| - | [[Category: Petsko, G | + | [[Category: Petsko, G A.]] |
[[Category: Ringe, D.]] | [[Category: Ringe, D.]] | ||
| - | [[Category: Stone, E | + | [[Category: Stone, E M.]] |
| - | [[Category: Thomas, P | + | [[Category: Thomas, P W.]] |
[[Category: GOL]] | [[Category: GOL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: zinc]] | [[Category: zinc]] | ||
| - | ''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 16:24:24 2008'' |
Revision as of 14:24, 21 February 2008
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1.6 Angstrom Resolution Structure of the Quorum-Quenching N-Acyl Homoserine Lactone Hydrolase of Bacillus thuringiensis
Overview
The three-dimensional structure of the N-acyl-l-homoserine lactone hydrolase (AHL lactonase) from Bacillus thuringiensis has been determined, by using single-wavelength anomalous dispersion (SAD) phasing, to 1.6-angstroms resolution. AHLs are produced by many Gram-negative bacteria as signaling molecules used in quorum-sensing pathways that indirectly sense cell density and regulate communal behavior. Because of their importance in pathogenicity, quorum-sensing pathways have been suggested as potential targets for the development of novel therapeutics. Quorum-sensing can be disrupted by enzymes evolved to degrade these lactones, such as AHL lactonases. These enzymes are members of the metallo-beta-lactamase superfamily and contain two zinc ions in their active sites. The zinc ions are coordinated to a number of ligands, including a single oxygen of a bridging carboxylate and a bridging water/hydroxide ion, thought to be the nucleophile that hydrolyzes the AHLs to ring-opened products, which can no longer act as quorum signals.
About this Structure
2A7M is a Single protein structure of sequence from Bacillus thuringiensis serovar kurstaki with and as ligands. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of the quorum-quenching N-acyl homoserine lactone hydrolase from Bacillus thuringiensis., Liu D, Lepore BW, Petsko GA, Thomas PW, Stone EM, Fast W, Ringe D, Proc Natl Acad Sci U S A. 2005 Aug 16;102(33):11882-7. Epub 2005 Aug 8. PMID:16087890
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