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VS核酶的折叠与催化作用。

Folding and catalysis by the VS ribozyme.

作者信息

Lafontaine Daniel A, Norman David G, Lilley David M J

机构信息

Cancer Research UK Nucleic Acid Structure Research Group, Department of Biochemistry, MSI/WTB Complex, The University of Dundee, UK.

出版信息

Biochimie. 2002 Sep;84(9):889-96. doi: 10.1016/s0300-9084(02)01406-2.

DOI:10.1016/s0300-9084(02)01406-2
PMID:12458081
Abstract

The VS ribozyme is a 154 nt self-cleaving RNA molecule that can be divided into a trans-acting five-helix ribozyme and stem-loop substrate. The structure of the ribozyme is organised by two three-way helical junctions, the structure of which has been determined by a combination of comparative gel electrophoresis and fluorescence resonance energy transfer experiments. From this, the overall global architecture of the ribozyme has been deduced. The substrate is then thought to dock into the cleft formed between helices II and VI, where it makes a close interaction with the loop containing A730. The A730 loop is the probable active site of the ribozyme, and A756 within it is a strong candidate to play a direct role in the transesterification chemistry, possibly by general acid-base catalysis.

摘要

VS核酶是一种154个核苷酸的自我切割RNA分子,可分为反式作用的五螺旋核酶和茎环底物。核酶的结构由两个三向螺旋连接点组成,其结构已通过比较凝胶电泳和荧光共振能量转移实验相结合的方法确定。由此推导出了核酶的整体全局结构。然后认为底物对接进入螺旋II和VI之间形成的裂隙中,在那里它与包含A730的环紧密相互作用。A730环可能是核酶的活性位点,其中的A756很可能在酯交换化学反应中发挥直接作用,可能是通过一般酸碱催化。

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Folding and catalysis by the VS ribozyme.VS核酶的折叠与催化作用。
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