Open AccessThe purification, crystallization and preliminary structural characterization of PhzM, a phenazine‐modifying methyltransferase from Pseudomonas aeruginosa
Author(s) -
Gohain Neelakshi,
Thomashow Linda S.,
Mavrodi Dmitri V.,
Blankenfeldt Wulf
Publication year - 2006
Publication title -
acta crystallographica section f
Language(s) - English
Resource type - Journals
ISSN - 1744-3091
DOI - 10.1107/s1744309106029149
Subject(s) - phenazine , pyocyanin , pseudomonas aeruginosa , chemistry , enzyme , dimer , spinach , stereochemistry , pseudomonas , biochemistry , bacteria , biology , organic chemistry , virulence , quorum sensing , genetics , gene
Pyocyanin, phenazine‐1‐carboxylic acid and more than 70 related compounds collectively known as phenazines are produced by various species of Pseudomonas , including the fluorescent pseudomonad P. aeruginosa , a Gram‐negative opportunistic pathogen in humans and animals. P. aeruginosa synthesizes a characteristic blue water‐soluble compound called pyocyanin (1‐hydroxy‐5‐methyl‐phenazine). Two enzymes designated PhzM and PhzS are involved in the terminal steps of its synthesis and very little is known about these enzymes. In this study, PhzM, a dimeric S ‐adenosylmethionine‐dependent methyltransferase, was purified and crystallized from PEG 3350/sodium cacodylate/sodium citrate pH 6.5. The crystals belong to space group P 1, with unit‐cell parameters a = 46.1, b = 61.8, c = 69.6 Å, α = 96.3, β = 106.6, γ = 106.9°. They contain one dimer in the asymmetric unit and diffract to a resolution of 1.8 Å. Anomalous data to 2.3 Å resolution have been collected from seleno‐ l ‐methionine‐labelled PhzM.