Abstract
THE three-dimensional structure of RNase H from Escherichia coli was determined at 1.8 Å resolution by X-ray crystallography. The enzyme was found to belong to the α + β class of structures, consisting of two distinct domains. The structure implies a possible region interacting with a DNA–RNA hybrid. The Mg2+-binding site essential for activity is located near a cluster of four acidic amino acids— one glutamic and three aspartic acid residues. These residues are completely conserved in the homology alignment of sequences of RNase H and reverse transcriptases from retro viruses and retrovirus-like entities1,2. The structural motif of β strands around the Mg2+-binding site has similarities to that in DNase I3–6.
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Katayanagi, K., Miyagawa, M., Matsushima, M. et al. Three-dimensional structure of ribonuclease H from E. coli. Nature 347, 306–309 (1990). https://doi.org/10.1038/347306a0
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DOI: https://doi.org/10.1038/347306a0
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