Three-dimensional structure of ribonuclease H from E. coli View Full Text


Ontology type: schema:ScholarlyArticle     


Article Info

DATE

1990-09

AUTHORS

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

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. More... »

PAGES

306-309

Identifiers

URI

http://scigraph.springernature.com/pub.10.1038/347306a0

DOI

http://dx.doi.org/10.1038/347306a0

DIMENSIONS

https://app.dimensions.ai/details/publication/pub.1000097890

PUBMED

https://www.ncbi.nlm.nih.gov/pubmed/1698262


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