Article
A dispensable peptide from Acidithiobacillus ferrooxidans tryptophanyl-tRNA synthetase affects tRNA binding.
FEBS letters - 18 Dec 2002
Zúñiga Roberto, Salazar Juan, Canales Mauricio, Orellana Omar
Abstract excerpt
The activation domain of class I aminoacyl-tRNA synthetases, which contains the Rossmann fold and the signature sequences HIGH and KMSKS, is generally split into two halves by the connective peptides (CP1, CP2) whose amino acid sequences are idiosyncratic. CP1 has been shown to participate in the binding of tRNA as well as the editing of the reaction intermediate aminoacyl-AMP or the aminoacyl-tRNA. No function...
Topics
- Adenosine Triphosphate
- Cloning, Molecular
- Escherichia coli
- Gammaproteobacteria
- Gene Deletion
- Genetic Complementation Test
- Kinetics
- Models, Genetic
- Mutation
- Peptides
- Protein Binding
- Protein Structure, Tertiary
- RNA, Transfer
- Recombinant Proteins
- Time Factors