Crystal Structure of a Non-discriminating Glutamyl-tRNA Synthetase

• Published in: Journal of molecular biology Vol. 361; no. 5; pp. 888 - 897
• Main Authors: Schulze, Jörg O., Masoumi, Ava, Nickel, Daniel, Jahn, Martina, Jahn, Dieter, Schubert, Wolf-Dieter, Heinz, Dirk W.
• Format: Journal Article
• Language: English
• Published: England Elsevier Ltd 01.09.2006
• Subjects: Amino Acid Sequence; aminoacylation; Anticodon - metabolism; anticodon recognition; Binding Sites; Catalysis; Crystallography, X-Ray; Cyanobacteria - enzymology; Glutamate-tRNA Ligase - chemistry; Glutamic Acid - metabolism; glutaminyl-tRNA synthetase; misacylation; mischarging; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Structure, Tertiary; Thermosynechococcus elongatus; Thermus thermophilus; D; Tth; CP; AdT; Eco; SC; misacylation; glutaminyl-tRNA synthetase; ND; anticodon recognition; Tel; aminoacylation; mischarging; AARS

Error-free protein biosynthesis is dependent on the reliable charging of each tRNA with its cognate amino acid. Many bacteria, however, lack a glutaminyl-tRNA synthetase. In these organisms, tRNA Gln is initially mischarged with glutamate by a non-discriminating glutamyl-tRNA synthetase (ND-GluRS)....