2000•Acta Crystallographica Section D Biological CrystallographyRequires access

Crystallization and preliminary X-ray diffraction studies of a monooxygenase fromStreptomyces coelicolorA3(2) involved in the biosynthesis of the polyketide actinorhodin

Steven G. Kendrew, Luca Federici, Carmelinda Savino, Adriana Erica Miele, E. Neil G. Marsh, Beatrice Vallone

Open publisher page 9 citations

Abstract

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.

About this research paper

What this paper is about

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.

Why it matters

OpenAlex reports 9 citations for this work. Citation counts describe recorded attention and do not establish research quality.

Key contribution

A contribution statement is not available in the OpenAlex record.

Method / approach

Method details are not available in the OpenAlex metadata.

Main findings

Findings are not separately available in the OpenAlex metadata.

Limitations

Limitations are not available in the OpenAlex metadata.

Applications

Application details are not available in the OpenAlex metadata.

Available abstract

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.

Key concepts: Actinorhodin, Streptomyces coelicolor, Polyketide, Biosynthesis, Stereochemistry, Streptomyces, Crystallization, Chemistry

Related papers

Back to paper searchBrowse research topicsOriginal source
Crystallization and preliminary X-ray diffraction studies of a monooxygenase fromStreptomyces coelicolorA3(2) involved in the biosynthesis of the polyketide actinorhodin — Research Paper | ScholarLens