Crystallization and X-ray diffraction of a halogenating enzyme, tryptophan 7-halogenase, from Pseudomonas fluorescens

Dong, Changjiang, Kotzsch, Alexander, Dorward, Mark, van Pée, Karl Heinz and Naismith, James H (2004) Crystallization and X-ray diffraction of a halogenating enzyme, tryptophan 7-halogenase, from Pseudomonas fluorescens. Acta Crystallographica Section D: Biological Crystallography, 60 (Pt 8). pp. 1438-40. ISSN 0907-4449

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Abstract

Chlorination of natural products is often required for their biological activity; notable examples include vancomycin, the last-ditch antibiotic. It is now known that many chlorinated natural products are made not by haloperoxidases, but by FADH2-dependent halogenases. The mechanism of the flavin-containing enzymes is obscure and there are no structural data. Here, crystals of PrnA (tryptophan 7-halogenase), an enzyme that regioselectively chlorinates tryptophan, cocrystallized with tryptophan and FAD are reported. The crystals belong to the tetragonal space group P4(3)2(1)2 or P4(1)2(1)2, with unit-cell parameters a = b = 67.8, c = 276.9 A. A data set to 1.8 A with 93% completeness and an Rmerge of 7.1% has been collected from a single flash-cooled crystal. A method for incorporating selenomethionine in a Pseudomonas fluorescens expression system also is reported.

Item Type: Article
Uncontrolled Keywords: crystallization,crystallography, x-ray,molecular structure,oxidoreductases,pseudomonas fluorescens,pyrrolnitrin
Faculty \ School: Faculty of Medicine and Health Sciences > Norwich Medical School
Depositing User: Pure Connector
Date Deposited: 17 Nov 2014 12:56
Last Modified: 21 Apr 2020 23:36
URI: https://ueaeprints.uea.ac.uk/id/eprint/50992
DOI: 10.1107/S0907444904012521

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