1gtr
STRUCTURAL BASIS OF ANTICODON LOOP RECOGNITION BY GLUTAMINYL-TRNA SYNTHETASE
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| , resolution 2.5Å | |||||||
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| Ligands: | |||||||
| Activity: | Glutamine--tRNA ligase, with EC number 6.1.1.18 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
OverviewOverview
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.
About this StructureAbout this Structure
1GTR is a Single protein structure of sequence from Escherichia coli. The following page contains interesting information on the relation of 1GTR with [Aminoacyl-tRNA Synthetases]. Full crystallographic information is available from OCA.
ReferenceReference
Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase., Rould MA, Perona JJ, Steitz TA, Nature. 1991 Jul 18;352(6332):213-8. PMID:1857417
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