1N5V

Crystal structure of a Monooxygenase from the gene ActVA-Orf6 of Streptomyces coelicolor in complex with the ligand Nanaomycin D

Summary for 1N5V

• Entry DOI: 10.2210/pdb1n5v/pdb
• Related: 1LQ9 1N5Q 1N5S 1N5T
• Descriptor: ActVA-Orf6 monooxygenase, 7-HYDROXY-5-METHYL-3,3A,5,11B-TETRAHYDRO-1,4-DIOXA-CYCLOPENTA[A]ANTHRACENE-2,6,11-TRIONE (3 entities in total)
• Functional Keywords: monooxygenase, aromatic polyketides, actinorhodin, dihydrokalafungin, nanaomycin d, streptomyces coelicolor, oxidoreductase
• Biological source: Streptomyces coelicolor
• Total number of polymer chains: 2
• Total formula weight: 24257.10

Authors

Sciara, G.,Kendrew, S.G.,Miele, A.E.,Marsh, N.G.,Federici, L.,Malatesta, F.,Schimperna, G.,Savino, C.,Vallone, B. (deposition date: 2002-11-07, release date: 2003-01-14, Last modification date: 2024-02-14)

Primary citation

Sciara, G.,Kendrew, S.G.,Miele, A.E.,Marsh, N.G.,Federici, L.,Malatesta, F.,Schimperna, G.,Savino, C.,Vallone, B.
The structure of ActVA-Orf6, a novel type of monooxygenase involved in actinorhodin biosynthesis
Embo J., 22:205-215, 2003

PubMed 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 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.

PubMed: 12514126
DOI: 10.1093/emboj/cdg031

Experimental method

X-RAY DIFFRACTION (2.24 Å)