PMID:9437423

Citation	Nakatsu, T, Kato, H and Oda, J (1998) Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase. Nat. Struct. Biol. 5:15-9
Abstract	The crystal structure of E. coli asparagine synthetase has been determined by X-ray diffraction analysis at 2.5 A resolution. The overall structure of the enzyme is remarkably similar to that of the catalytic domain of yeast aspartyl-tRNA synthetase despite low sequence similarity. These enzymes have a common reaction mechanism that implies the formation of an aminoacyl-adenylate intermediate. The active site architecture and most of the catalytic residues are also conserved in both enzymes. These proteins have probably evolved from a common ancestor even though their sequence similarities are small. The functional and structural similarities of both enzymes suggest that new enzymatic activities would generally follow the recruitment of a protein catalyzing a similar chemical reaction.
Links	PubMed
Keywords	Amino Acid Sequence; Amino Acyl-tRNA Synthetases/ultrastructure; Aspartate-Ammonia Ligase/ultrastructure; Aspartic Acid/chemistry; Binding Sites; Crystallography, X-Ray; Escherichia coli/enzymology; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Structure, Secondary; Protein Structure, Tertiary; Saccharomyces cerevisiae/enzymology; Sequence Alignment; Sequence Homology, Amino Acid
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