Article
Structural analysis of the active site architecture of the VapC toxin from Shigella flexneri.
Proteins - 1 Jul 2016
Xu Kehan, Dedic Emil, Brodersen Ditlev E
Abstract excerpt
The VapC toxin from the Shigella flexneri 2a virulence plasmid pMYSH6000 belongs to the PIN domain protein family, which is characterized by a conserved fold with low amino acid sequence conservation. The toxin is a bona fide Mg(2+) -dependent ribonuclease and has been shown to target initiator tRNA(fMet) in vivo. Here, we present crystal structures of active site catalytic triad mutants D7A, D7N, and D98N of the...
Topics
- Bacterial Proteins
- Bacterial Toxins
- Catalytic Domain
- Crystallography, X-Ray
- Dysentery, Bacillary
- Humans
- Magnesium
- Models, Molecular
- Mutation
- Plasmids
- Protein Binding
- Protein Conformation