1n5q
From Proteopedia
Crystal structure of a Monooxygenase from the gene ActVA-Orf6 of Streptomyces coelicolor in complex with dehydrated Sancycline
Overview
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 components including a proton gate and an O(2)/H(2)O 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.
About this Structure
1N5Q is a Single protein structure of sequence from Streptomyces coelicolor. Full crystallographic information is available from OCA.
Reference
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis., Sciara G, Kendrew SG, Miele AE, Marsh NG, Federici L, Malatesta F, Schimperna G, Savino C, Vallone B, EMBO J. 2003 Jan 15;22(2):205-15. PMID:12514126 Page seeded by OCA on Sat May 3 02:07:34 2008
