Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
Structural basis of anticodon loop recognition by glutaminyl-tRNA synthetase
复制标题
谷氨酰胺酰-tRNA合成酶识别反密码子环的结构基础
作者：
M. A. Rould;J. Perona;T. Steitz
与转运RNAGln和ATP复合的大肠杆菌β-氨酰转运RNA合成酶的精细晶体结构表明，酶结合的tRNAGln的反密码子环的结构与未复合的tRNA分子的已知晶体结构有很大不同。反密码子茎由两个非沃森-克里克碱基对延伸，留下三个反密码子碱基未配对并展开以紧密结合到蛋白质中的三个独立互补口袋中。这些相互作用表明，整个反密码子环提供了重要的网站之间的tRNA分子的氨酰tRNA合成酶的歧视。
The refined crystal structure of Escherichia coli glutaminyl transfer RNA synthetase complexed with transfer RNAGln and ATP reveals that the struc-ture of the anticodon loop of the enzyme-bound tRNAGln differs extensively from that of the known crystal structures of uncomplexed tRNA molecules. The anticodon stem is extended by two non-Watson–Crick base pairs, leaving the three anti-codon bases unpaired and splayed out to bind snugly into three separate complementary pockets in the protein. These interactions suggest that the entire anticodon loop provides essential sites for glutaminyl tRNA synthetase discrimination among tRNA molecules.
影响因子：
5.6
作者：
YARUS, M;CLINE, SW;THOMPSON, RC
通讯作者：
THOMPSON, RC