書誌事項
- タイトル別名
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- Aminoacyl-tRNA Synthetase : Structural Basis for the Substrate Recognition and the Molecular Evolution
- アミノアシル t RNA ゴウセイ コウソ コウゾウテキ ケンチ カラ ミタ
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抄録
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.
収録刊行物
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- 日本結晶学会誌
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日本結晶学会誌 38 (1), 60-67, 1996
日本結晶学会
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詳細情報 詳細情報について
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- CRID
- 1390001204088601472
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- NII論文ID
- 10002024753
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- NII書誌ID
- AN00188364
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- ISSN
- 18845576
- 03694585
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- NDL書誌ID
- 3934772
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- データソース種別
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- JaLC
- NDL
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- 抄録ライセンスフラグ
- 使用不可