Nakatsu T, et al. (1998) Crystal structure of asparagine synthetase reveals a close evolutionary relationship to class II aminoacyl-tRNA synthetase. Nat Struct Biol 5(1):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.
|Status: Published||Type: Journal Article | Research Support, Non-U.S. Gov't||PubMed ID: 9437423|
Topics addressed in this paper
- To go to the Locus page for a gene, click on the gene name.
|Non-Fungal Related Genes/Proteins|
|Protein/Nucleic Acid Structure|