Nature. 1990 Sep 20;347(6290):306-9.

Three-dimensional structure of ribonuclease H from E. coli.

Katayanagi K, Miyagawa M, Matsushima M, Ishikawa M, Kanaya S, Ikehara M, Matsuzaki T, Morikawa K.

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Protein Engineering Research Institute, Osaka, Japan.

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.

PMID:: 1698262; [PubMed - indexed for MEDLINE]

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Structures reported by this article

Structural Details Of Ribonuclease H From Escherichia Coli As Refined To An Atomic Resolution

PDB: 2RN2

Source: Escherichia coli

Method: X-Ray Diffraction

Resolution: 1.48 Å

See all 18 structures...

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