Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1991-07

AUTHORS

M A Rould, J J Perona, T A Steitz

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. More... »

PAGES

213-218

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/352213a0

DOI

http://dx.doi.org/10.1038/352213a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1052831152

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1857417


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