Crystallization and preliminary X-ray diffraction studies of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of the polyketide actinorhodin.
The aromatic monooxygenase ActVA-Orf6 from Streptomyces coelicolor A3(2) that catalyses an unusual oxidation on the actinorhodin biosynthetic pathway has been crystallized. The crystals diffract to 1.73 A and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.95, b = 59.29, c = 71.67 A. Solvent-content (44%) and self-rotation function calculations predict the presence of two molecules in the asymmetric unit. Structure determination should provide further insight into the enzyme mechanism and aid in the design of biosynthetic pathways to produce new polyketide natural products with novel functionality.
Kendrew
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SG
Dipartimento di Scienze Biochimiche e Centro di Biologia Molecolare del CNR, Università di Roma 'La Sapienza', Piazzale Aldo Moro 5, 00185 Rome, Italy. steve.kendrew@biotica.co.uk
Federici
L
L
Savino
C
C
Miele
A
A
Marsh
E N
EN
Vallone
B
B
D000880:Anthraquinones / Q000378:metabolism; D000900:Anti-Bacterial Agents / Q000096:biosynthesis; D003460:Crystallization; D018360:Crystallography, X-Ray; D006899:Mixed Function Oxygenases / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism; D013302:Streptomyces / Q000201:enzymology*; D000095622:Benzoisochromanequinones
D000880:Anthraquinones; D000900:Anti-Bacterial Agents; D006899:Mixed Function Oxygenases; C013390:actinorhodin; D000095622:Benzoisochromanequinones