Open AccessPreliminary crystallographic characterization of PrnB, the second enzyme in the pyrrolnitrin biosynthetic pathway
Author(s) -
De Laurentis Walter,
Leang Khim,
Hahn Katrin,
Podemski Bianca,
Adam Ariane,
Kroschwald Sonja,
Carter Lester G.,
Van Pee KarlHeinz,
Naismith James H.
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106041649
Subject(s) - tryptophan , rhizoctonia solani , stereochemistry , pseudomonas fluorescens , fludioxonil , crystallography , chemistry , monomer , biochemistry , biology , amino acid , organic chemistry , botany , fungicide , bacteria , genetics , polymer
Pyrrolnitrin is the active ingredient of drugs for the treatment of superficial fungal infections and was used as a lead structure for the development of fludioxonil. It is an effective agent for plant diseases caused by the fungal pathogen Rhizoctonia solani . Pyrrolnitrin is made in four steps, the second of which, catalyzed by PrnB, is a novel chemical rearrangement of 7‐chlorotryptophan. PrnB was overproduced in Pseudomonas fluorescens (BL915) and well diffracting crystals were obtained of a triple cysteine‐to‐serine mutant by sitting‐drop vapour diffusion. Crystals grown in the presence of l ‐7‐chlorotryptophan, d ‐tryptophan and l ‐tryptophan are reported. Data sets for each are reported with high‐resolution limits of 2.0, 1.75 and 1.75 Å, respectively. Two crystals (PrnB in the presence of d ‐tryptophan and l ‐7‐chlorotryptophan) belong to space group C 2 with similar unit‐cell parameters ( a = 68.6, b = 79.5, c = 92.7 Å, α = γ = 90.0, β = 103.8°). Crystals grown in the presence of l ‐tryptophan belong to space group C 222 1 and have unit‐cell parameters a = 67.7, b = 80.1, c = 129.5 Å. All crystals contain a monomer in the asymmetric unit.