1rnh
From Proteopedia
(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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| - | [[Image:1rnh.jpg|left|200px]]<br /><applet load="1rnh" size=" | + | [[Image:1rnh.jpg|left|200px]]<br /><applet load="1rnh" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rnh, resolution 2.0Å" /> | caption="1rnh, resolution 2.0Å" /> | ||
'''STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br /> | '''STRUCTURE OF RIBONUCLEASE H PHASED AT 2 ANGSTROMS RESOLUTION BY MAD ANALYSIS OF THE SELENOMETHIONYL PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Ribonuclease H digests the RNA strand of duplex RNA.DNA hybrids into | + | 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== | ==About this Structure== | ||
| - | 1RNH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http:// | + | 1RNH is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [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] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RNH OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Ribonuclease H]] | [[Category: Ribonuclease H]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Crouch, R | + | [[Category: Crouch, R J.]] |
| - | [[Category: Hendrickson, W | + | [[Category: Hendrickson, W A.]] |
[[Category: Satow, Y.]] | [[Category: Satow, Y.]] | ||
[[Category: Yang, W.]] | [[Category: Yang, W.]] | ||
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[[Category: hydrolase(endoribonuclease)]] | [[Category: hydrolase(endoribonuclease)]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:52:46 2008'' |
Revision as of 12:52, 21 February 2008
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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 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
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