A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases
| Autor: | Mark A. Rould, Thomas A. Steitz, C. Landès, C. Zelwer, Simone Brunie, Jean-Loup Risler, John J. Perona |
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| Rok vydání: | 1995 |
| Předmět: |
chemistry.chemical_classification
Multiple sequence alignment Sequence Homology Amino Acid Aminoacyl tRNA synthetase Protein Conformation Molecular Sequence Data General Medicine Methionine-tRNA Ligase Biology Biochemistry Amino acid Amino Acyl-tRNA Synthetases chemistry.chemical_compound Protein structure Sequence homology chemistry Models Chemical Consensus sequence Escherichia coli Structure based Amino Acid Sequence Peptide sequence Sequence Alignment |
| Zdroj: | Biochimie. 77(3) |
| ISSN: | 0300-9084 |
| Popis: | 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. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
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