Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis.
Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis.
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DOI：
10.1146/annurev.biophys.27.1.475
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发表时间：
1998
期刊：
影响因子：
--
通讯作者：
J. Wedekind;David B. McKay
中科院分区：
文献类型：
--
作者：
J. Wedekind;David B. McKay
锤头状核酶是一种小的催化RNA，在依赖于二价金属离子的反应中裂解目标磷酸二酯键。锤头的晶体结构揭示了分子的酶“基态”的三重折叠；然而，它们并没有阐明核酶的催化机制，可能是因为需要显著的构象重排才能达到酶的过渡态。锤头中看到的结构域可以与转移和核糖体RNA中的序列或结构基序相关，这表明它们代表了在大型、复杂的RNA中发现的第三构建块。
The hammerhead ribozyme is a small catalytic RNA that cleaves a target phosphodiester bond in a reaction dependent on divalent metal ions. Crystal structures of the hammerhead reveal the tertiary fold of an enzymatic "ground state" of the molecule; however, they do not clarify the catalytic mechanism of the ribozyme, presumably because a significant conformational rearrangement is required to reach an enzymatic transition state. The structural domains seen in the hammerhead can be related to sequence or structural motifs in transfer and ribosomal RNAs, suggesting that they represent tertiary building blocks that will be found in large, complex RNAs.