1RNH

Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein.

(1990) Science 249: 1398-1405

• PubMed: 2169648 Search on PubMed
• DOI: https://doi.org/10.1126/science.2169648
• Primary Citation of Related Structures:  
  1RNH


• PubMed Abstract: 
  

  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.

   View More

---

Organizational Affiliation: 

Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.