3. 新しいタンパク質立体構造 アミノアシルtRNA合成酵素 : 構造的見地から見た基質認識機構と分子進化 [in Japanese] Aminoacyl-tRNA Synthetase : Structural Basis for the Substrate Recognition and the Molecular Evolution [in Japanese]
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Aminoacyl-tRNA synthetases (aaRS's) play key roles in the correct protein biosynthesis through strict recognition/ligation of the cognate amino acid and tRNA. Twenty aaRS's were evolutionally devided into two classes (class I and class II) based on the architecture of the ATP-binding domain. Our recent result on the crystal structure of class-I aaRS (glutamyl-tRNA synthetase) delineates that aaRS's accomplish their strict recognition of the tRNA through a combination of insertions and deletions of modular structures in the class/subclass-defining domains and a total exchange of the non-conserved anticodon-binding domains. In contrast, structure of ternary complex of aaRS ·ATP ·amino-acid suggests that the strict amino-acid recognition is accomplished through evolutionary accumulation of mutation of the amino acid residues in the amino-acid binding site.
X-RAYS 38(1), 60-67, 1996-02-28
The Crystallographic Society of Japan