A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases.
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.
Landès
C
C
Centre de Génétique Moléculaire, Université P & M Curie, Gif-sur-Yvette, France.
Perona
J J
JJ
Brunie
S
S
Rould
M A
MA
Zelwer
C
C
Steitz
T A
TA
Risler
J L
JL
D000595:Amino Acid Sequence; D000604:Amino Acyl-tRNA Synthetases / Q000737:chemistry* / Q000145:classification; D004926:Escherichia coli / Q000737:chemistry / Q000201:enzymology; D008718:Methionine-tRNA Ligase / Q000737:chemistry; D008956:Models, Chemical; D008969:Molecular Sequence Data; D011487:Protein Conformation; D016415:Sequence Alignment / Q000145:classification*; D017386:Sequence Homology, Amino Acid
D000604:Amino Acyl-tRNA Synthetases; D008718:Methionine-tRNA Ligase