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Structural homology in the amino-terminal domains of two aminoacyl-tRNA synthetases.
J Mol Biol ; 171(4): 571-6, 1983 Dec 25.
Article em En | MEDLINE | ID: mdl-6363712
The three-dimensional structures of two animoacyl-tRNA synthetases, the methionyl-tRNA synthetase from Escherichia coli (MetRS) and the tyrosyl-tRNA synthetase from Bacillus stearothermophilus (TyrRS), show a remarkable similarity over a span of about 140 amino acids. The region of homologous folding corresponds to a five-stranded parallel beta-sheet, including a mononucleotide-binding fold. One cysteine and two histidine residues that were found to be invariant in the amino acid sequences occupy similar places in the nucleotide-binding fold. In TyrRS, these residues are close to the adenylate binding site, and in MetRS to the Mg2+-ATP binding site.
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tirosina-tRNA Ligase / Aminoacil-tRNA Sintetases / Metionina tRNA Ligase Idioma: En Revista: J Mol Biol Ano de publicação: 1983 Tipo de documento: Article
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Coleções: 01-internacional Base de dados: MEDLINE Assunto principal: Tirosina-tRNA Ligase / Aminoacil-tRNA Sintetases / Metionina tRNA Ligase Idioma: En Revista: J Mol Biol Ano de publicação: 1983 Tipo de documento: Article