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 Angstrom) 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 components including a proton gate and an O-2/H2O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure.

The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis / Sciara, Giuliano; S. G., Kendrew; Miele, Adriana Erica; N. G., Marsh; L., Federici; Malatesta, Francesco; G., Schimperna; L., Savino; Vallone, Beatrice. - In: EMBO JOURNAL. - ISSN 0261-4189. - 22:2(2003), pp. 205-215. [10.1093/emboj/cdg031]

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

SCIARA, Giuliano;MIELE, Adriana Erica;MALATESTA, FRANCESCO;VALLONE, Beatrice
2003

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 Angstrom) 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 components including a proton gate and an O-2/H2O gate with a putative protein channel. This is the first crystal structure of an enzyme involved in the tailoring of a type II aromatic polyketide and illustrates some of the enzyme-substrate recognition features that may apply to a range of other enzymes involved in modifying a polyketide core structure.
2003
actinorhodin; monooxygenase; monooxygenases; polyketide; polyketides; protein structure; streptomyces coelicolor
01 Pubblicazione su rivista::01a Articolo in rivista
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis / Sciara, Giuliano; S. G., Kendrew; Miele, Adriana Erica; N. G., Marsh; L., Federici; Malatesta, Francesco; G., Schimperna; L., Savino; Vallone, Beatrice. - In: EMBO JOURNAL. - ISSN 0261-4189. - 22:2(2003), pp. 205-215. [10.1093/emboj/cdg031]
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Utilizza questo identificativo per citare o creare un link a questo documento: https://hdl.handle.net/11573/249876
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