Abstract
The crystal structure of E. coli asparagine synthetase has been determined by X-ray diffraction analysis at 2.5 Å 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 activites would generally follow the recruitment of a protein catalyzing a similiar chemical reaction.
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Nakatsu, T., Kato, H. & Oda, J. Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase. Nat Struct Mol Biol 5, 15–19 (1998). https://doi.org/10.1038/nsb0198-15
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DOI: https://doi.org/10.1038/nsb0198-15
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