Grum-Tokars Valerie, Milovanovic Michael, Wedekind Joseph E
The Department of Biochemistry and Molecular Biology, FUHS/The Chicago Medical School, 3333 Green Bay Road, North Chicago, Illinois 60064, USA.
Acta Crystallogr D Biol Crystallogr. 2003 Jan;59(Pt 1):142-5. doi: 10.1107/s0907444902019066. Epub 2002 Dec 19.
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 & Ferré-D'Amaré (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 A. Complete diffraction data have been collected to 3.35 A resolution. Structural analysis should provide details of intermolecular RNA docking, including the ground-state conformations of the U(39)C mutation relevant to hairpin catalysis.
发夹状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，它们对接形成具有生物活性的酶。此前，发夹状核酶的晶体结构已被解析为一种四链螺旋连接体，其中包含U1A蛋白作为人工晶体堆积基序[鲁珀特和费雷-达马雷（2001年），《自然》（伦敦），410，780 - 786]。在此，报道了在无蛋白质情况下最小的无连接头发夹状核酶64聚体的结晶情况。晶体在空间群P6(1)22中生长，晶胞参数a = 93.1，c = 123.2 Å。已收集到分辨率为3.35 Å的完整衍射数据。结构分析应能提供分子间RNA对接的详细信息，包括与发夹状核酶催化相关的U(39)C突变的基态构象。
