Article
A metal-binding motif implicated in RNA recognition by an aminoacyl-tRNA synthetase and by a retroviral gene product.
Molecular microbiology - 1 May 1992
Miller W T, Schimmel P
Abstract excerpt
A randomly generated mutation in Escherichia coli alanine tRNA synthetase compensates for a mutation in its cognate tRNA. The enzyme's mutation occurs next to a Cys-X2-Cys-X6-His-X2-His metal-binding motif that is distinct from the zinc finger motif found in some DNA-binding proteins. Instead, the synthetase's metal binding domain resembles the Cys-X2-Cys-X4-His-X4-Cys metal-binding domain of the gag gene product...
Topics
- Alanine-tRNA Ligase
- Allosteric Regulation
- Allosteric Site
- Amino Acid Sequence
- Bacterial Proteins
- Cobalt
- Consensus Sequence
- Escherichia coli
- Gene Products, gag
- Genes, Bacterial
- Genes, gag
