95 溶液中におけるリボヌクレアーゼHの立体構造解析(ポスター発表の部)

概要

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Ribonuclease H is a enzyme which cleaves the RNA part of an RNA-DNA hybrid duplex. Assignments of the main and side chain's NMR signals of the enzyme from Escherichia coli, consisting of 155 amino acid residues (17.6kDa), were completed on ^1H, ^<15>N and ^<13>C nuclei by 2D and 3D NMR experiments. Thus, the secondary structures in solution were determined as five β-strands forming a sheet and the five α-helices, which were compatible with the structure proposed with X-ray crystallography. It's three dimensional structure was determined by the so-called distance analysis, which matched with the distance and angle constraints obtained from NOE data. NMR compatible structures have been calculated with the DADAS90 program equiped in the MolSkop system (JEOL). The comparison of the three dimensinal structures in solution and in crystal has revealed significant aspects in the enzymatic function.
天然有機化合物討論会の論文
1993-09-10