The hairpin ribozyme: from crystal structure to function.
The hairpin ribozyme: from crystal structure to function.
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发夹核酶：从晶体结构到功能。
DOI：
10.1042/bst0301105
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发表时间：
2002
影响因子：
3.9
通讯作者：
Rupert,PB
中科院分区：
文献类型：
--
作者：
Ferré-D'amaré,AR;Rupert,PB
发夹核酶是已知的四种天然催化 RNA 之一，可对 RNA 进行序列特异性切割。它具有特别的生化意义，因为与“经典”核酶（例如 I 组内含子）不同，它似乎不使用金属离子作为催化辅因子。我们以 2.4 Å 的分辨率确定了发夹-核酶-抑制剂复合物的晶体结构。核酶的活性位点由两个不规则双螺旋对接产生。对接导致螺旋的主要结构重排，包括底物链的扭曲，使其形成反应性构象。这种 RNA 酶是否完全依赖结合能进行催化，或者是否采用了其他机制，例如一般酸碱催化，仍有待确定。
The hairpin ribozyme is one of four known natural catalytic RNAs that carry out sequence-specific cleavage of RNA. It is of particular biochemical interest because, unlike ‘classic’ ribozymes, such as the group I intron, it appears not to employ metal ions as catalytic cofactors. We have determined the crystal structure of a hairpin-ribozyme-inhibitor complex at a resolution of 2.4 Å. The active site of the ribozyme results from docking of two irregular double helices. Docking results in major structural rearrangements of the helices, including a distortion of the substrate strand that brings it into a reactive conformation. It remains to be established whether this RNA enzyme relies exclusively on binding energy to carry out catalysis, or whether some other mechanism, such as general acid-base catalysis, is being employed.