Abstract
RNase H binds RNA-DNA hybrid and double-stranded RNA (dsRNA) duplexes with similar affinity, but only cleaves the RNA in the former. To potentially gain insight into the conformational origins of substrate recognition by the enzyme from Escherichia coli, cocrystallization experiments were carried out with RNase HI-dsRNA (enzyme-inhibitor) complexes. Crystals were obtained of two complexes containing 9-mer and 10-mer RNA duplexes that diffracted X-rays to 3.5 and 4 A resolution, respectively.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Research Support, U.S. Gov't, Non-P.H.S.
MeSH terms
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Crystallography, X-Ray
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Escherichia coli / chemistry*
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Escherichia coli / enzymology
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Escherichia coli / genetics
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RNA, Double-Stranded / chemistry*
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RNA, Double-Stranded / genetics
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RNA, Double-Stranded / metabolism
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Ribonuclease H / chemistry*
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Ribonuclease H / genetics
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Ribonuclease H / metabolism
Substances
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RNA, Double-Stranded
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Ribonuclease H
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ribonuclease HI