Skip to main content

Overexpression, purification and crystallization of PhzA, the first enzyme of the phenazine biosynthesis pathway of Pseudomonas fluorescens 2-79

Buy Article:

$43.00 plus tax (Refund Policy)

Phenazines are broad-spectrum antibiotic metabolites produced by organisms such as Pseudomonas and Streptomyces. Phenazines have been shown to enhance microbial competitiveness and the pathogenic potential of the organisms that synthesize them. PhzA (163 residues, approximate molecular weight 18.7 kDa) is the product of the first of seven genes of the operon responsible for phenazine biosynthesis in P. fluorescens 2-79. This enzyme is thought to catalyse one of the final steps in the formation of phenazine-1-carboxylic acid, the end product of phenazine biosynthesis in P. fluorescens 2–79. Here, the purification and crystallization of recombinant PhzA are reported. Crystals diffracting to 2.1 Å were obtained using 1.6 M magnesium sulfate and 2-morpholinoethanesulfonic acid monohydrate (MES) buffer pH 5.2–5.6. Crystals of both native and seleno-l-methionine-labelled protein belong to the orthorhombic space group P212121, with unit-cell parameters a = 66.8, b = 75.3, c = 84.5 Å. The asymmetric unit contains one dimer of PhzA.
No References
No Citations
No Supplementary Data
No Data/Media
No Metrics

Keywords: PhzA; phenazine biosynthesis

Document Type: Research Article

Publication date: 2004-06-01

  • Access Key
  • Free content
  • Partial Free content
  • New content
  • Open access content
  • Partial Open access content
  • Subscribed content
  • Partial Subscribed content
  • Free trial content
Cookie Policy
Cookie Policy
Ingenta Connect website makes use of cookies so as to keep track of data that you have filled in. I am Happy with this Find out more