Site-Directed Mutagenesis and Preliminary X-Ray Crystallographic Studies of the Tabtoxin Resistance Protein

Title: Site-Directed Mutagenesis and Preliminary X-Ray Crystallographic Studies of the Tabtoxin Resistance Protein

Volume: 10 Issue: 3

Author(s): Yi Ding, Shentao Li, Xiaofeng Li, Fei Sun, Jinyuan Liu, Nanming Zhao and Zihe Rao

Affiliation:

Keywords: tabtoxin resistance protein, mutation, crystallization, circular dichroism spectra, dynamic light scattering

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.

Cite this article as:

Ding Yi, Li Shentao, Li Xiaofeng, Sun Fei, Liu Jinyuan, Zhao Nanming and Rao Zihe, Site-Directed Mutagenesis and Preliminary X-Ray Crystallographic Studies of the Tabtoxin Resistance Protein, Protein & Peptide Letters 2003; 10 (3) . https://dx.doi.org/10.2174/0929866033478924