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Science 21 September 1990:
Vol. 249. no. 4975, pp. 1398 - 1405
DOI: 10.1126/science.2169648
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Articles
Science, Vol 249, Issue 4975, 1398-1405
Copyright © 1990 by American Association for the Advancement of Science
Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein
W Yang,
WA Hendrickson,
RJ Crouch,
and
Y Satow
Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.
Ribonuclease H digests the RNA strand of duplex RNA.DNA hybrids into oligonucleotides. This activity is indispensable for retroviral infection and is involved in bacterial replication. The ribonuclease H from Escherichia coli is homologous with the retroviral proteins. The crystal structure of the E. coli enzyme reveals a distinctive alpha-beta tertiary fold. Analysis of the molecular model implicates a carboxyl triad in the catalytic mechanism and suggests a likely mode for the binding of RNA.DNA substrates. The structure was determined by the method of multiwavelength anomalous diffraction (MAD) with the use of synchrotron data from a crystal of the recombinant selenomethionyl protein.
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