1IPS

ISOPENICILLIN N SYNTHASE FROM ASPERGILLUS NIDULANS (MANGANESE COMPLEX)

1IPS の概要

• エントリーDOI: 10.2210/pdb1ips/pdb
• 分子名称: ISOPENICILLIN N SYNTHASE, MANGANESE (II) ION (3 entities in total)
• 機能のキーワード: b-lactam antibiotic, oxygenase, penicillin biosynthesis, antibiotic biosynthesis, oxidoreductase
• 由来する生物種: Emericella nidulans
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 75347.42

構造登録者

Roach, P.L.,Clifton, I.J.,Fulop, V.,Harlos, K.,Barton, G.J.,Hajdu, J.,Andersson, I.,Schofield, C.J.,Baldwin, J.E. (登録日: 1997-03-21, 公開日: 1998-03-25, 最終更新日: 2024-02-07)

主引用文献

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

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: 7791906
DOI: 10.1038/375700a0

実験手法

X-RAY DIFFRACTION (2.5 Å)