Crystallization and X-ray diffraction analysis of an all-RNA U39C mutant of the minimal hairpin ribozyme
Crystallization and X-ray diffraction analysis of an all-RNA U39C mutant of the minimal hairpin ribozyme
复制标题
DOI：
10.1107/s0907444902019066
复制
发表时间：
2003-01-01
期刊：
影响因子：
--
通讯作者：
Wedekind, JE
中科院分区：
文献类型：
--
作者：
Grum-Tokars, V;Milovanovic, M;Wedekind, JE
发夹核酶是一种天然存在的催化RNA，由两个螺旋-环-螺旋结构域A和B组成，它们对接形成生物活性酶。以前，发夹的晶体结构已被解析为四向螺旋连接，其掺入U1 A蛋白作为人工晶体包装基序[鲁珀特和Ferre-D' Amare（2001），Nature（伦敦），410，780-786]。在这里，一个最小的无连接发夹核酶64聚体的结晶报告在蛋白质的情况下。晶体生长在P6（1）22空间群，晶胞参数a = 93.1，c = 123.2埃。完整的衍射数据已收集到3.35埃的分辨率。结构分析应提供分子间RNA对接的细节，包括与发夹催化相关的U39 C突变的基态构象。
The hairpin ribozyme is a naturally occurring catalytic RNA composed of two helix-loop-helix domains, A and B, that dock to form the biologically active enzyme. Previously, the crystal structure of the hairpin has been solved as a four-way helical junction that incorporated the U1A protein as an artificial crystal-packing motif [Rupert & Ferre-D' Amare (2001), Nature (London), 410, 780-786]. Here, the crystallization of a minimal junctionless hairpin ribozyme 64-mer is reported in the absence of protein. Crystals grow in space group P6(1)22, with unit-cell parameters a = 93.1, c = 123.2 Angstrom. Complete diffraction data have been collected to 3.35 Angstrom resolution. Structural analysis should provide details of intermolecular RNA docking, including the ground-state conformations of the U39C mutation relevant to hairpin catalysis.