Crystal structure of a bacterial ribonuclease P RNA
Crystal structure of a bacterial ribonuclease P RNA
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DOI：
10.1073/pnas.0506662102
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发表时间：
2005-09-20
影响因子：
11.1
通讯作者：
Pace, NR
中科院分区：
文献类型：
--
作者：
Kazantsev, AV;Krivenko, AA;Pace, NR
来自嗜热脂肪芽孢杆菌（Bacilius stearothermophilus）的417-nt核糖核酸酶P RNA的X射线晶体结构被解析到3.3埃分辨率。这种RNA酶由许多通过局部和远程相互作用连接在一起的同轴堆叠的螺旋结构域构成。这些螺旋结构域排列形成一个非常平坦的表面，这是由大量的生化数据在转移RNA底物的前体的结合和切割暗示。以前的光亲和交联数据被用来定位基板上的晶体结构，并确定的核酶的化学活性位点。该位点位于高度保守的核心结构中，该核心结构由螺旋间序列之间错综复杂的交织长距离相互作用形成。
The x-ray crystal structure of a 417-nt ribonuclease P RNA from Bacilius stearothermophilus was solved to 3.3-angstrom resolution. This RNA enzyme is constructed from a number of coaxially stacked helical domains joined together by local and long-range interactions. These helical domains are arranged to forma remarkably flat surface, which is implicated by a wealth of biochemical data in the binding and cleavage of the precursors of transfer RNA substrate. Previous photoaffinity crosslinking data are used to position the substrate on the crystal structure and to identify the chemically active site of the ribozyme. This site is located in a highly conserved core structure formed by intricately interlaced long-range interactions between interhelical sequences.