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Specific sequence homology and three-dimensional structure of an aminoacyl transfer RNA synthetase.
- Source :
-
Science (New York, N.Y.) [Science] 1984 Dec 14; Vol. 226 (4680), pp. 1315-7. - Publication Year :
- 1984
-
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.
Details
- Language :
- English
- ISSN :
- 0036-8075
- Volume :
- 226
- Issue :
- 4680
- Database :
- MEDLINE
- Journal :
- Science (New York, N.Y.)
- Publication Type :
- Academic Journal
- Accession number :
- 6390679
- Full Text :
- https://doi.org/10.1126/science.6390679