The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis.

ABSTRACT: ActVA-Orf6 monooxygenase from Streptomyces coelicolor that catalyses the oxidation of an aromatic intermediate of the actinorhodin biosynthetic pathway is a member of a class of small monooxygenases that carry out oxygenation without the assistance of any of the prosthetic groups, metal ions or cofactors normally associated with activation of molecular oxygen. The overall structure is a ferredoxin-like fold with a novel dimeric assembly, indicating that the widely represented ferredoxin fold may sustain yet another functionality. The resolution (1.3 A) of the enzyme structure and its complex with substrate and product analogues allows us to visualize the mechanism of binding and activation of the substrate for attack by molecular oxygen, and utilization of two gates for the reaction compon

SUBMITTER: Sciara G 

PROVIDER: S-EPMC140106 | biostudies-literature | 2003 Jan

REPOSITORIES: biostudies-literature