Crystallization and preliminary X-ray diffraction studies of a monooxygenase from Streptomyces coelicolor A3(2) involved in the biosynthesis of the polyketide actinorhodin

被引:8
作者
Kendrew, SG
Federici, L
Savino, C
Miele, A
Marsh, ENG
Vallone, B
机构
[1] Univ Roma La Sapienza, Dipartimento Sci Biochim, I-00185 Rome, Italy
[2] Univ Roma La Sapienza, CNR, Ctr Biol Mol, I-00185 Rome, Italy
[3] Biot Technol Ltd, Cambridge CB3 0DJ, England
[4] Univ Michigan, Dept Chem, Ann Arbor, MI 48109 USA
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2000年 / 56卷
关键词
D O I
10.1107/S0907444900001189
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
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 Angstrom and belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 46.95, b = 59.29, c = 71.67 Angstrom. 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.
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页码:481 / 483
页数:3
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