Loukachevitch Lioudmila V, Egli Martin
Department of Biochemistry, School of Medicine, Vanderbilt University, Nashville, Tennessee 37232, USA.
Acta Crystallogr Sect F Struct Biol Cryst Commun. 2007 Feb 1;63(Pt 2):84-8. doi: 10.1107/S1744309106055461. Epub 2007 Jan 17.
RNase H binds RNA-DNA hybrid and double-stranded RNA (dsRNA) duplexes with similar affinity, but only cleaves the RNA in the former. To potentially gain insight into the conformational origins of substrate recognition by the enzyme from Escherichia coli, cocrystallization experiments were carried out with RNase HI-dsRNA (enzyme-inhibitor) complexes. Crystals were obtained of two complexes containing 9-mer and 10-mer RNA duplexes that diffracted X-rays to 3.5 and 4 A resolution, respectively.
核糖核酸酶H以相似的亲和力结合RNA-DNA杂交双链体和双链RNA(dsRNA)双链体,但仅切割前者中的RNA。为了深入了解来自大肠杆菌的该酶对底物识别的构象起源,进行了核糖核酸酶HI-dsRNA(酶-抑制剂)复合物的共结晶实验。获得了两种分别含有9聚体和10聚体RNA双链体的复合物晶体,其X射线衍射分辨率分别为3.5埃和4埃。