PMID:6390679
| Citation |
Webster, T, Tsai, H, Kula, M, Mackie, GA and Schimmel, P (1984) Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase. Science 226:1315-7 |
|---|---|
| Abstract |
Few and limited amino acid sequence homologies have been found among eight bacterial aminoacyl transfer RNA (tRNA) synthetases whose primary structures are known. The entire 939-amino acid primary structure of Escherichia coli isoleucyl-tRNA synthetase is now reported. In a sequence of 11 consecutive amino acids matching a sequence in E. coli methionyl-tRNA synthetase, there are ten identical residues and one conservative change. This is the strongest homology recorded between any two aminoacyl tRNA synthetases. This part of the methionine enzyme's three-dimensional structure has been determined, and it occurs in a mononucleotide binding fold; a close three-dimensional structural homology of this part of the enzyme with Bacillus stearothermophilus tyrosyl-tRNA synthetase has also been reported. The three synthetases probably fold identically in this region. |
| Links | |
| Keywords |
Amino Acid Sequence; Amino Acyl-tRNA Synthetases; Escherichia coli/enzymology; Geobacillus stearothermophilus/enzymology; Isoleucine-tRNA Ligase; Methionine-tRNA Ligase; Protein Conformation |
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