1rnh
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(New page: 200px<br /><applet load="1rnh" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rnh, resolution 2.0Å" /> '''STRUCTURE OF RIBONUCL...)
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Revision as of 23:36, 20 November 2007
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STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN
Overview
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.
About this Structure
1RNH is a Single protein structure of sequence from [1] with SO4 as ligand. Active as Ribonuclease H, with EC number 3.1.26.4 Full crystallographic information is available from OCA.
Reference
Structure of ribonuclease H phased at 2 A resolution by MAD analysis of the selenomethionyl protein., Yang W, Hendrickson WA, Crouch RJ, Satow Y, Science. 1990 Sep 21;249(4975):1398-405. PMID:2169648
Page seeded by OCA on Wed Nov 21 01:43:51 2007
