2a7m: Difference between revisions

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==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.

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==

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[[Category: Single protein]]

[[Category: Fast, W.]]

[[Category: Lepore, B.W.]]

[[Category: Lepore, B W.]]

[[Category: Liu, D.]]

[[Category: Petsko, G.A.]]

[[Category: Petsko, G A.]]

[[Category: Ringe, D.]]

[[Category: Stone, E.M.]]

[[Category: Stone, E M.]]

[[Category: Thomas, P.W.]]

[[Category: Thomas, P W.]]

[[Category: GOL]]

[[Category: ZN]]

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[[Category: zinc]]

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@@ Line 4: / Line 4: @@
 ==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.
+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==
@@ Line 14: / Line 14: @@
 [[Category: Single protein]]
 [[Category: Fast, W.]]
-[[Category: Lepore, B.W.]]
+[[Category: Lepore, B W.]]
 [[Category: Liu, D.]]
-[[Category: Petsko, G.A.]]
+[[Category: Petsko, G A.]]
 [[Category: Ringe, D.]]
-[[Category: Stone, E.M.]]
+[[Category: Stone, E M.]]
-[[Category: Thomas, P.W.]]
+[[Category: Thomas, P W.]]
 [[Category: GOL]]
 [[Category: ZN]]
@@ Line 30: / Line 30: @@
 [[Category: zinc]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jan 29 17:56:13 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:24:24 2008''