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1rnh
From Proteopedia
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[[Image:1rnh.jpg|left|200px]] | [[Image:1rnh.jpg|left|200px]] | ||
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'''STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN''' | '''STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN''' | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1RNH is a [[Single protein]] structure | + | 1RNH is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RNH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Satow, Y.]] | [[Category: Satow, Y.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
| - | + | ''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 | + | |
Revision as of 04:42, 3 May 2008
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. 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 Sat May 3 07:42:03 2008
