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锤头状核酶的晶体结构:与核酶折叠及催化作用的关系

Crystallographic structures of the hammerhead ribozyme: relationship to ribozyme folding and catalysis.

作者信息

Wedekind J E, McKay D B

机构信息

Department of Structural Biology, Stanford University School of Medicine, California 94305-5126, USA.

出版信息

Annu Rev Biophys Biomol Struct. 1998;27:475-502. doi: 10.1146/annurev.biophys.27.1.475.

Abstract

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.

摘要

锤头状核酶是一种小的催化性RNA,它在依赖二价金属离子的反应中切割靶磷酸二酯键。锤头状核酶的晶体结构揭示了该分子酶促“基态”的三级折叠;然而,它们并未阐明核酶的催化机制,推测这是因为需要显著的构象重排才能达到酶促过渡态。在锤头状核酶中观察到的结构域可能与转移RNA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RNA中会发现的三级结构单元。

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