2a7m
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2a7m |SIZE=350|CAPTION= <scene name='initialview01'>2a7m</scene>, resolution 1.60Å | |PDB= 2a7m |SIZE=350|CAPTION= <scene name='initialview01'>2a7m</scene>, resolution 1.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= aiia ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29339 Bacillus thuringiensis serovar kurstaki]) | |GENE= aiia ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=29339 Bacillus thuringiensis serovar kurstaki]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2a7m FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2a7m OCA], [http://www.ebi.ac.uk/pdbsum/2a7m PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2a7m RCSB]</span> | ||
}} | }} | ||
| Line 29: | Line 32: | ||
[[Category: Stone, E M.]] | [[Category: Stone, E M.]] | ||
[[Category: Thomas, P W.]] | [[Category: Thomas, P W.]] | ||
| - | [[Category: GOL]] | ||
| - | [[Category: ZN]] | ||
[[Category: bimetallo di-zinc]] | [[Category: bimetallo di-zinc]] | ||
[[Category: bimetallohydrolase]] | [[Category: bimetallohydrolase]] | ||
| Line 39: | Line 40: | ||
[[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 Mon Mar 31 01:48:54 2008'' |
Revision as of 22:48, 30 March 2008
| |||||||
| , resolution 1.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Gene: | aiia (Bacillus thuringiensis serovar kurstaki) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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
Page seeded by OCA on Mon Mar 31 01:48:54 2008
