1hl7
GAMMA LACTAMASE FROM AN AUREOBACTERIUM SPECIES IN COMPLEX WITH 3A,4,7,7A-TETRAHYDRO-BENZO [1,3] DIOXOL-2-ONE
OverviewOverview
The structure of the recombinant (-) gamma-lactamase from an Aureobacterium species has been solved at 1.73A resolution in the cubic space group F23 with unit cell parameters a=b=c=240.6A. The trimeric enzyme has an alpha/beta hydrolase fold and closely resembles the cofactor free haloperoxidases. The structure has been solved in complex with a covalently bound ligand originating from the host cell and also in the unligated form. The associated density in the former structure has been interpreted as the two-ring ligand (3aR,7aS)-3a,4,7,7a-tetrahydro-benzo [1,3] dioxol-2-one which forms a tetrahedral complex with OG of the catalytic Ser98. Soaks of these crystals with the industrial substrate gamma-lactam or its structural analogue, norcamphor, result in the displacement of the ligand from the enzyme active site, thereby allowing determination of the unligated structure. The presence of the ligand in the active site protects the enzyme from serine hydrolase inhibitors. Cyclic ethylene carbonate, the first ring of the ligand, was shown to be a substrate of the enzyme.
About this StructureAbout this Structure
1HL7 is a Single protein structure of sequence from Microbacterium. Full crystallographic information is available from OCA.
ReferenceReference
The crystal structure of a (-) gamma-lactamase from an Aureobacterium species reveals a tetrahedral intermediate in the active site., Line K, Isupov MN, Littlechild JA, J Mol Biol. 2004 Apr 30;338(3):519-32. PMID:15081810 Page seeded by OCA on Fri May 2 18:58:19 2008