YEAST ASPARTYL-TRANSFER-RNA SYNTHETASE - A STRUCTURAL VIEW OF THE AMINOACYLATION REACTION

被引：14

作者：

CAVARELLI, J ^{[1
]}

REES, B ^{[1
]}

THIERRY, JC ^{[1
]}

MORAS, D ^{[1
]}

机构：

[1] CNRS, INST BIOL MOLEC & CELLULAIRE, BIOL STRUCT LAB, UPR 9004, F-67084 STRASBOURG, FRANCE

来源：

BIOCHIMIE | 1993年 / 75卷 / 12期

关键词：

ASPARTYL-TRANSFER-RNA SYNTHETASE; TRANSFER-RNA; ATP; AMINOACYLATION; CRYSTAL STRUCTURE;

D O I：

10.1016/0300-9084(93)90011-G

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

The refinement of the crystal structure of a binary complex formed by yeast AspRS and tRNA(Asp) provided a detailed understanding of the recognition of tRNA by an aminoacyl-tRNA synthetase. The crystal structures of several complexes containing ATP, alone or with aspartic acid, were also determined and refined. These studies led to a complete description of the active site of the enzyme and to the elucidation of the location and interactions of the various substrates. Based on these structural results, a class II specific pathway for the aminoacylation reaction can be proposed.

引用

页码：1117 / 1123

页数：7

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