doi: 10.1038/347306a0.
Three-dimensional structure of ribonuclease H from E. coli
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- PMID: 1698262
- DOI: 10.1038/347306a0
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Three-dimensional structure of ribonuclease H from E. coli
Nature.
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Abstract
The three-dimensional structure of RNase H from Escherichia coli was determined at 1.8 A resolution by X-ray crystallography. The enzyme was found to belong to the alpha + beta 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 retroviruses and retrovirus-like entities. The structural motif of beta strands around the Mg2(+)-binding site has similarities to that in DNase I.
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