2oqc
From Proteopedia
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Crystal Structure of Penicillin V acylase from Bacillus subtilis
Overview
Penicillin acylase proteins are amidohydrolase enzymes that cleave, penicillins at the amide bond connecting the side chain to their, beta-lactam nucleus. An unannotated protein from Bacillus subtilis has, been expressed in Escherichia coli, purified and confirmed to possess, penicillin V acylase activity. The protein was crystallized using the, hanging-drop vapour-diffusion method from a solution containing 4 M sodium, formate in 100 mM Tris-HCl buffer pH 8.2. Diffraction data were collected, under cryogenic conditions to a spacing of 2.5 A. The crystals belonged to, the orthorhombic space group C222(1), with unit-cell parameters a = 111.0, b = 308.0, c = 56.0 A. The estimated Matthews coefficient was 3.23 A3, Da(-1), corresponding to 62% solvent content. The structure has been, solved using molecular-replacement methods with B. sphaericus penicillin V, acylase (PDB code 2pva) as the search model.
About this Structure
2OQC is a Single protein structure of sequence from Bacillus subtilis. Active as Penicillin amidase, with EC number 3.5.1.11 Full crystallographic information is available from OCA.
Reference
Cloning, purification, crystallization and preliminary structural studies of penicillin V acylase from Bacillus subtilis., Rathinaswamy P, Pundle AV, Prabhune AA, Sivaraman H, Brannigan JA, Dodson GG, Suresh CG, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2005 Jul 1;61(Pt, 7):680-3. Epub 2005 Jun 15. PMID:16511127
Page seeded by OCA on Wed Jan 23 11:06:14 2008
