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Literature summary for 6.1.1.1 extracted from

  • Paukstelis, P.J.; Chari, N.; Lambowitz, A.M.; Hoffman, D.
    NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase that functions in group I intron splicing (2011), Biochemistry, 50, 3816-3826.
    View publication on PubMedView publication on EuropePMC

Cloned(Commentary)

Cloned (Comment) Organism
expression of C-terminal domain of TyrRS in Escherichia coli strain BL21(DE3) Aspergillus nidulans

Protein Variants

Protein Variants Comment Organism
additional information interaction analysis of deletion and truncation mutants, overview Aspergillus nidulans

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
Aspergillus nidulans 5739
-

Organism

Organism UniProt Comment Textmining
Aspergillus nidulans
-
-
-

Purification (Commentary)

Purification (Comment) Organism
recombinant C-terminal domain from Escherichia coli strain BL21(DE3) by cation exchange chromatography and gel filtration Aspergillus nidulans

Subunits

Subunits Comment Organism
dimer three-dimensional structures of subunits A and B, modelling, overview Aspergillus nidulans
More NMR structure of the C-terminal domain of a tyrosyl-tRNA synthetase, modeling of the C-terminal domain/group I intron interactions, overview Aspergillus nidulans

Synonyms

Synonyms Comment Organism
Tyrosyl-tRNA synthetase
-
Aspergillus nidulans
TyrRS
-
Aspergillus nidulans
YTS
-
Aspergillus nidulans

General Information

General Information Comment Organism
physiological function tyrosyl-tRNA synthetase functions in group I intron splicing Aspergillus nidulans