Site-directed mutagenesis and preliminary x-ray crystallographic studies of the tabtoxin resistance protein

Protein Pept Lett. 2003 Jun;10(3):255-63. doi: 10.2174/0929866033478924.

Abstract

Tabtoxin resistance protein (TTR) is an enzyme that catalyzes the acetylation of tabtoxin rendering tabtoxin-producing pathogens tolerant to their own phytotoxins. According to the structure based detoxification mechanism of TTR, three site-directed mutants Y141F, D130N and Y141F-D130N were constructed and overexpressed in E. coli. The products were then purified and their properties were analyzed by CD and DLS. Crystallization trials of two mutants Y141F andY141F-D130N were preformed.

Publication types

  • Comparative Study
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Acetylation
  • Acetyltransferases / chemistry*
  • Acetyltransferases / genetics*
  • Bacterial Proteins*
  • Circular Dichroism
  • Crystallization
  • Crystallography, X-Ray / methods*
  • Escherichia coli / genetics
  • Escherichia coli / metabolism
  • Inactivation, Metabolic
  • Isoelectric Point
  • Mutagenesis, Site-Directed*
  • Mutation / genetics*
  • Pseudomonas / genetics
  • Pseudomonas / metabolism*
  • Recombinant Proteins / chemistry
  • Recombinant Proteins / isolation & purification
  • Recombinant Proteins / metabolism
  • Solubility

Substances

  • Bacterial Proteins
  • Recombinant Proteins
  • Acetyltransferases
  • tabtoxin-resistance protein, Pseudomonas syringae