1ips
From Proteopedia
|
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)
Overview
Penicillin antibiotics are all produced from fermentation-derived, penicillins because their chemical synthesis is not commercially viable., The key step in penicillin biosynthesis, in which both the beta-lactam and, thiazolidine rings of the nucleus are created, is mediated by, isopenicillin N synthase (IPNS), which binds ferrous iron and uses, dioxygen as a cosubstrate. In a unique enzymatic step, with no chemical, precedent, IPNS catalyses the transfer of four hydrogen atoms from its, tripeptide substrate to dioxygen forming, in a single reaction, the, complete bicyclic nucleus of the penicillins. We now report the structure, of IPNS complexed with manganese, which reveals the active site is, unusually buried within a 'jelly-roll' motif and lined by hydrophobic, residues, and suggest how this structure permits the process of penicillin, formation. Sequence analyses indicate IPNS, 1-aminocyclopropane-1-carboxylic acid oxidase and many of the, 2-oxo-acid-dependent oxygenases contain a conserved jelly-roll motif, forming a new structural family of enzymes.
About this Structure
1IPS is a Single protein structure of sequence from Emericella nidulans with MN as ligand. Structure known Active Sites: SA and SB. Full crystallographic information is available from OCA.
Reference
Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes., Roach PL, Clifton IJ, Fulop V, Harlos K, Barton GJ, Hajdu J, Andersson I, Schofield CJ, Baldwin JE, Nature. 1995 Jun 22;375(6533):700-4. PMID:7791906
Page seeded by OCA on Mon Nov 5 14:58:49 2007
