1rnh

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{{STRUCTURE_1rnh| PDB=1rnh | SCENE= }}
{{STRUCTURE_1rnh| PDB=1rnh | SCENE= }}
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'''STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''
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===STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN===
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==Overview==
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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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(as it appears on PubMed at http://www.pubmed.gov), where 2169648 is the PubMed ID number.
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{{ABSTRACT_PUBMED_2169648}}
==About this Structure==
==About this Structure==
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[[Category: Satow, Y.]]
[[Category: Satow, Y.]]
[[Category: Yang, W.]]
[[Category: Yang, W.]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:42:03 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 06:14:36 2008''

Revision as of 03:14, 29 July 2008

Image:1rnh.png

Template:STRUCTURE 1rnh

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

Template:ABSTRACT PUBMED 2169648

About this Structure

1RNH is a Single protein structure. 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 Tue Jul 29 06:14:36 2008

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