Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution
Structure of protein L7Ae bound to a K-turn derived from an archaeal box H/ACA sRNA at 1.8 Å resolution
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DOI：
10.1016/j.str.2004.03.015
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发表时间：
2004-05-01
期刊：
影响因子：
5.7
通讯作者：
Ferré-D'Amaré, AR
中科院分区：
文献类型：
--
作者：
Hamma, T;Ferré-D'Amaré, AR
古细菌RNA结合蛋白L7 Ae及其真核同源物15.5 kDa/Snu 13识别K-turns。这个结构基序通常由两个词干组成（一个是串联的A（.）G碱基对，另一个与沃森-克里克对）由一个不对称的内环连接。L7 Ae识别核糖体和盒C/D RNA中的常规K-转角，但也特异性结合末端茎环处的一些盒H/ACA RNA。这些有A（.）G配对茎，但缺少Watson-Crick茎。詹氏甲烷球菌L7 Ae与对称双链RNA结合而没有沃森-克里克茎的结构证明了如何仅用A（）构建不同核糖核蛋白复合物的该组分的结合位点。G茎和环。RNA在碱基三联体和二价阳离子的紧密结合的帮助下采用功能构象。与15.5 kDa/Snu 13-RNA复合物结构的比较表明了为什么真核同源物不识别末端茎环L7 Ae结合位点。
The archaeal RNA binding protein L7Ae and its eukaryotic homolog 15.5 kDa/Snu13 recognize K-turns. This structural motif is canonically comprised of two stems (one with tandem A(.)G base pairs, the other with Watson-Crick pairs) linked by an asymmetric internal loop. L7Ae recognizes conventional K-turns in ribosomal and box C/D RNAs but also binds specifically to some box H/ACA RNAs at terminal stem loops. These have the A(.)G paired stem, but lack the Watson-Crick stem. The structure of Methanococcus jannaschii L7Ae bound to a symmetric duplex RNA without Watson-Crick stems demonstrates how a binding site for this component of diverse ribonucleoprotein complexes can be constructed with only the A(.)G stem and the loop. The RNA adopts a functional conformation with the aid of a base triple and tight binding of divalent cations. Comparison with the 15.5 kDa/Snu13-RNA complex structure suggests why the eukaryotic homolog does not recognize terminal stem loop L7Ae binding sites.