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A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases.
- Source :
-
Biochimie [Biochimie] 1995; Vol. 77 (3), pp. 194-203. - Publication Year :
- 1995
-
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.
- Subjects :
- Amino Acid Sequence
Amino Acyl-tRNA Synthetases classification
Escherichia coli chemistry
Escherichia coli enzymology
Methionine-tRNA Ligase chemistry
Models, Chemical
Molecular Sequence Data
Protein Conformation
Sequence Homology, Amino Acid
Amino Acyl-tRNA Synthetases chemistry
Sequence Alignment classification
Subjects
Details
- Language :
- English
- ISSN :
- 0300-9084
- Volume :
- 77
- Issue :
- 3
- Database :
- MEDLINE
- Journal :
- Biochimie
- Publication Type :
- Academic Journal
- Accession number :
- 7647112
- Full Text :
- https://doi.org/10.1016/0300-9084(96)88125-9