Article
Role for a conserved structural motif in assembly of a class I aminoacyl-tRNA synthetase active site.
Biochemistry - 8 Feb 2011
Casina Veronica C, Lobashevsky Andrew A, McKinney William E, Brown Cassidy L, Alexander Rebecca W
Abstract excerpt
The catalytic domains of class I aminoacyl-tRNA synthetases are built around a conserved Rossmann nucleotide binding fold, with additional polypeptide domains responsible for tRNA binding or hydrolytic editing of misacylated substrates. Structural comparisons identified a conserved motif bridging the catalytic and anticodon binding domains of class Ia and Ib enzymes. This stem contact fold (SCF) has been proposed...
Topics
- Amino Acid Motifs
- Amino Acid Sequence
- Catalytic Domain
- Conserved Sequence
- Escherichia coli
- Escherichia coli Proteins
- Kinetics
- Methionine-tRNA Ligase
- Molecular Sequence Data
- Mutation
- Protein Folding
- Protein Structure, Secondary
- Sequence Alignment