Article
Substitution of proline 82 by threonine induces autophosphorylating activity in GTP-binding domain of elongation factor Tu.
The Journal of biological chemistry - 25 Apr 1990
Cool R H, Jensen M, Jonák J, Clark B F, Parmeggiani A
Abstract excerpt
Mutation of Pro82 into Thr, a residue situated in the second element (D80CPG83) of the consensus sequence proposed to interact with GTP/GDP in GTP-binding proteins was introduced via site-directed mutagenesis in the isolated guanine nucleotide-binding domain (G domain) of elongation factor Tu. G...
Topics
- Base Sequence
- Binding Sites
- Cytidine Diphosphate
- GTP Phosphohydrolase-Linked Elongation Factors
- Guanosine Triphosphate
- Kinetics
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Oligonucleotide Probes
- Peptide Elongation Factor Tu
- Peptide Mapping
- Phosphoric Monoester Hydrolases
- Phosphorylation
- Plasmids
- Proline
- Protein Conformation
- Recombinant Proteins