文章基本信息

标题：NMR Structure of Ribonuclease HI from Escherichia coli
本地全文：下载
作者：Masako FUJIWARA ; Toshiyo KATO ; Toshio YAMAZAKI 等
期刊名称：Biological and Pharmaceutical Bulletin
印刷版ISSN：0918-6158
电子版ISSN：1347-5215
出版年度：2000
卷号：23
期号：10
页码：1147-1152
DOI：10.1248/bpb.23.1147
出版社：The Pharmaceutical Society of Japan
摘要：The solution structure of ribonuclease HI (RNase HI) from Escherichia coli (E. coli), a protein of 155 residues, was determined. Three-dimensional nuclear Overhauser enhancement spectroscopy (NOESY) was used to obtain 1424 distance constraints between individually assigned polypeptide chain hydrogen atoms. Supplemental geometric constraints of 90φ angles and 12_χ1 angles, and the distance constraints of 66 hydrogen bonds were experimentally derived. Using the DADAS90 program that calculates structures in dihedral angle space, 15 structures satisfying almost all constraints were obtained. The average root mean square deviation (RMSD) from the mean structure was 0.75Å for backbone atoms. The RMSD for backbone atoms between the representative NMR structure with the smallest constraint violation and crystal structures was within 1.2Å. Although the NMR and crystal structures thus resemble one another, a significant discrepancy was observed in a region termed 'basic protrusion.' The discrepancy observed in NMR experiments is explained by fluctuation in this region.
关键词：ribonuclease H;NOE;solution structure;distance geometry