Crystallization and preliminary X-ray analysis of Escherichia coli RNase HI-dsRNA complexes.
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.
Loukachevitch
Lioudmila V
LV
Department of Biochemistry, School of Medicine, Vanderbilt University, Nashville, Tennessee 37232, USA.
Egli
Martin
M
D018360:Crystallography, X-Ray; D004926:Escherichia coli / Q000737:chemistry* / Q000201:enzymology / Q000235:genetics; D012330:RNA, Double-Stranded / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D016914:Ribonuclease H / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism
D012330:RNA, Double-Stranded; D016914:Ribonuclease H; C078856:ribonuclease HI