Summary information and primary citation
- PDB-id
-
1gtr;
DSSR-derived features in text and
JSON formats; DNAproDB
- Class
- complex (ligase-trna)
- Method
- X-ray (2.5 Å)
- Summary
- Structural basis of anticodon loop recognition by
glutaminyl-trna synthetase
- Reference
-
Rould MA, Perona JJ, Steitz TA (1991): "Structural
basis of anticodon loop recognition by glutaminyl-tRNA
synthetase." Nature, 352,
213-218. doi: 10.1038/352213a0.
- Abstract
- The refined crystal structure of Escherichia coli
glutaminyl transfer RNA synthetase complexed with transfer
RNA(Gln) and ATP reveals that the structure of the
anticodon loop of the enzyme-bound tRNA(Gln) differs
extensively from that of the known crystal structures of
uncomplexed tRNA molecules. The anticodon stem is extended
by two non-Watson-Crick base pairs, leaving the three
anti-codon bases unpaired and splayed out to bind snugly
into three separate complementary pockets in the protein.
These interactions suggest that the entire anticodon loop
provides essential sites for glutaminyl tRNA synthetase
discrimination among tRNA molecules.
