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- W2093808216 abstract "The superimposable dinucleotide fold domains of MetRS, GlnRS and TyrRS define structurally equivalent amino acids which have been used to constrain the sequence alignments of the 10 class I aminoacyl-tRNA synthetases (aaRS). The conservation of those residues which have been shown to be critical in some aaRS enables to predict their location and function in the other synthetases, particularly: i) a conserved negatively-charged residue which binds the alpha-amino group of the amino acid substrate; ii) conserved residues within the inserted domain bridging the two halves of the dinucleotide-binding fold; and iii) conserved residues in the second half of the fold which bind the amino acid and ATP substrate. The alignments also indicate that the class I synthetases may be partitioned into two subgroups: a) MetRS, IleRS, LeuRS, ValRS, CysRS and ArgRS; b) GlnRS, GluRS, TyrRS and TrpRS." @default.
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- W2093808216 date "1995-01-01" @default.
- W2093808216 modified "2023-10-18" @default.
- W2093808216 title "A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases" @default.
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- W2093808216 doi "https://doi.org/10.1016/0300-9084(96)88125-9" @default.
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