(Q27650929)

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Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase

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Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase (English)

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author name string

M A Rould

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J J Perona

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T A Steitz

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language of work or name

English

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publication date

18 July 1991

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published in

Nature

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volume

352

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issue

6332

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page(s)

213-8

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cites work

In vitro conversion of a methionine to a glutamine-acceptor tRNA.

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https://api.crossref.org/works/10.1038%2F352213A0

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Aminoacyl tRNA synthetases: general scheme of structure-function relationships in the polypeptides and recognition of transfer RNAs

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A single mutational modification of a tryptophan-specific transfer RNA permits aminoacylation by glutamine and translation of the codon UAG

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7 January 2021

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Structure of E. coli glutaminyl-tRNA synthetase complexed with tRNA(Gln) and ATP at 2.8 A resolution

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Crystallographic refinement by simulated annealing. Application to a 2.8 A resolution structure of aspartate aminotransferase.

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Structure of yeast phenylalanine tRNA at 3 Å resolution

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https://api.crossref.org/works/10.1038%2F352213A0

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7 January 2021

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Crystal structure of yeast tRNAAsp

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Crystal structure of yeast phenylalanine transfer RNA. II. Structural features and functional implications

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Restrained refinement of two crystalline forms of yeast aspartic acid and phenylalanine transfer RNA crystals

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Three-dimensional structure of Escherichia coli initiator tRNAfMet

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Solution conformation of an RNA hairpin loop

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Actions of the anticodon arm in translation on the phenotypes of RNA mutants.

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Relaxation of a transfer RNA specificity by removal of modified nucleotides

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Involvement of the anticodon region of Escherichia coli tRNAGln and tRNAGlu in the specific interaction with cognate aminoacyl-tRNA synthetase. Alteration of the 2-thiouridine derivatives located in the anticodon of the tRNAs by BrCN or sulfur depri

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Compilation of tRNA sequences and sequences of tRNA genes

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Structural basis for misaminoacylation by mutant E. coli glutaminyl-tRNA synthetase enzymes

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7 January 2021

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Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase

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Partition of tRNA synthetases into two classes based on mutually exclusive sets of sequence motifs

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Crystallographic study at 2.5 A resolution of the interaction of methionyl-tRNA synthetase from Escherichia coli with ATP.

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Identifiers

DOI

10.1038/352213A0

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Dimensions Publication ID

1052831152

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PubMed publication ID

1857417

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