STRUCTURE OF RIBONUCLEASE-H PHASED AT 2-A RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
STRUCTURE OF RIBONUCLEASE-H PHASED AT 2-A RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
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DOI：
10.1126/science.2169648
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发表时间：
1990-09-21
期刊：
影响因子：
56.9
通讯作者：
SATOW, Y
中科院分区：
文献类型：
--
作者：
YANG, W;HENDRICKSON, WA;SATOW, Y
核糖核酸酶H将双链RNA的RNA链消化成寡核苷酸。这种活性对于逆转录病毒感染是必不可少的，并参与细菌复制。来自大肠杆菌的核糖核酸酶H与逆转录病毒蛋白是同源的。大肠杆菌酶的晶体结构显示出独特的α - β。第三折。分子模型的分析暗示了催化机制中的羧基三联体，并提出了RNA.cntdot.DNA底物结合的可能模式。采用多波长异常衍射（MAD）法和同步加速器数据对重组硒甲硫基蛋白晶体进行了结构测定。
Ribonuclease H digests the RNA strand of duplex RNA.cntdot.DNA hybrids into oligonucleotides. This activity is indispensable for retroviral infection and is involved in bacterial replication. The ribonuclease H from Escherichia coli is homologous with the retroviral proteins. The crystal structure of the E. coli enzyme reveals a distinctive .alpha.-.beta. tertiary fold. Analysis of the molecular model implicates a carboxyl triad in the catalytic mechanism and suggests a likely mode for the binding of RNA.cntdot.DNA substrates. The structure was determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the recombinant selenomethionyl protein.