1rnh
From Proteopedia
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|PDB= 1rnh |SIZE=350|CAPTION= <scene name='initialview01'>1rnh</scene>, resolution 2.0Å | |PDB= 1rnh |SIZE=350|CAPTION= <scene name='initialview01'>1rnh</scene>, resolution 2.0Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene> | + | |LIGAND= <scene name='pdbligand=MSE:SELENOMETHIONINE'>MSE</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Ribonuclease_H Ribonuclease H], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.26.4 3.1.26.4] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1rnh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rnh OCA], [http://www.ebi.ac.uk/pdbsum/1rnh PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1rnh RCSB]</span> | ||
}} | }} | ||
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[[Category: Satow, Y.]] | [[Category: Satow, Y.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
| - | [[Category: SO4]] | ||
[[Category: hydrolase(endoribonuclease)]] | [[Category: hydrolase(endoribonuclease)]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:30:30 2008'' |
Revision as of 20:30, 30 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Ribonuclease H, with EC number 3.1.26.4 | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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]. 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
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