1RNH

STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN

Summary for 1RNH

• Entry DOI: 10.2210/pdb1rnh/pdb
• Descriptor: RIBONUCLEASE HI, SULFATE ION (3 entities in total)
• Functional Keywords: hydrolase(endoribonuclease)
• Biological source: Escherichia coli
• Cellular location: Cytoplasm (Potential): P00647
• Total number of polymer chains: 1
• Total formula weight: 17906.64

Authors

Yang, W.,Hendrickson, W.A.,Crouch, R.J.,Satow, Y. (deposition date: 1990-07-11, release date: 1991-10-15, Last modification date: 2024-10-23)

Primary citation

Yang, W.,Hendrickson, W.A.,Crouch, R.J.,Satow, Y.
Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein.
Science, 249:1398-1405, 1990

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.

PubMed: 2169648

Experimental method

X-RAY DIFFRACTION (2 Å)