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A structure-based multiple sequence alignment of all class I aminoacyl-tRNA synthetases.
Landès, C; Perona, J J; Brunie, S; Rould, M A; Zelwer, C; Steitz, T A; Risler, J L.
Afiliação
  • Landès C; Centre de Génétique Moléculaire, Université P & M Curie, Gif-sur-Yvette, France.
Biochimie ; 77(3): 194-203, 1995.
Article em En | MEDLINE | ID: mdl-7647112
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.
Assuntos
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Alinhamento de Sequência / Aminoacil-tRNA Sintetases Tipo de estudo: Prognostic_studies Idioma: En Revista: Biochimie Ano de publicação: 1995 Tipo de documento: Article País de afiliação: França
Buscar no Google
Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Alinhamento de Sequência / Aminoacil-tRNA Sintetases Tipo de estudo: Prognostic_studies Idioma: En Revista: Biochimie Ano de publicação: 1995 Tipo de documento: Article País de afiliação: França