1IPS
ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)
Summary for 1IPS
| Entry DOI | 10.2210/pdb1ips/pdb |
| Descriptor | ISOPENICILLIN N SYNTHASE, MANGANESE (II) ION (3 entities in total) |
| Functional Keywords | b-lactam antibiotic, oxygenase, penicillin biosynthesis, antibiotic biosynthesis, oxidoreductase |
| Biological source | Emericella nidulans |
| Total number of polymer chains | 2 |
| Total formula weight | 75347.42 |
| Authors | Roach, P.L.,Clifton, I.J.,Fulop, V.,Harlos, K.,Barton, G.J.,Hajdu, J.,Andersson, I.,Schofield, C.J.,Baldwin, J.E. (deposition date: 1997-03-21, release date: 1998-03-25, Last modification date: 2024-02-07) |
| Primary citation | Roach, P.L.,Clifton, I.J.,Fulop, V.,Harlos, K.,Barton, G.J.,Hajdu, J.,Andersson, I.,Schofield, C.J.,Baldwin, J.E. Crystal structure of isopenicillin N synthase is the first from a new structural family of enzymes. Nature, 375:700-704, 1995 Cited by PubMed Abstract: 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. PubMed: 7791906DOI: 10.1038/375700a0 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.5 Å) |
Structure validation
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