Article
Mutation and evolution of the magnesium-binding site of a class II aminoacyl-tRNA synthetase.
Biochemistry - 8 Jun 2004
Ador Laurent, Jaeger Sophie, Geslain Renaud, Martin Franck, Cavarelli Jean, Eriani Gilbert
Abstract excerpt
Aminoacyl-tRNA synthetases contain one or three Mg(2+) ions in their catalytic sites. In addition to their role in ATP binding, these ions are presumed to play a role in catalysis by increasing the electropositivity of the alpha-phosphate and stabilizing the pentavalent transition state. In the class II aaRS, two highly conserved carboxylate residues have been shown to participate with Mg(2+) ions in binding and...
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