1rpl
From Proteopedia
(New page: 200px<br /><applet load="1rpl" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rpl, resolution 2.3Å" /> '''2.3 ANGSTROMS CRYSTAL...) |
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| - | [[Image:1rpl.jpg|left|200px]]<br /><applet load="1rpl" size=" | + | [[Image:1rpl.jpg|left|200px]]<br /><applet load="1rpl" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rpl, resolution 2.3Å" /> | caption="1rpl, resolution 2.3Å" /> | ||
'''2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA'''<br /> | '''2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The crystal structure of the catalytic domain of rat DNA polymerase beta | + | The crystal structure of the catalytic domain of rat DNA polymerase beta (pol beta) has been determined at 2.3 A resolution and refined to an R factor of 0.22. The mixed alpha/beta protein has three subdomains arranged in an overall U shape reminiscent of other polymerase structures. The folding topology of pol beta, however, is unique. Two divalent metals bind near three aspartic acid residues implicated in the catalytic activity. In the presence of Mn2+ and dTTP, interpretable electron density is seen for two metals and the triphosphate, but not the deoxythymidine moiety. The principal interaction of the triphosphate moiety is with the bound divalent metals. |
==About this Structure== | ==About this Structure== | ||
| - | 1RPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http:// | + | 1RPL is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RPL OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Almassy, R | + | [[Category: Almassy, R J.]] |
| - | [[Category: II, J | + | [[Category: II, J F.Davies.]] |
[[Category: nucleotidyltransferase]] | [[Category: nucleotidyltransferase]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:53:17 2008'' |
Revision as of 12:53, 21 February 2008
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2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA
Overview
The crystal structure of the catalytic domain of rat DNA polymerase beta (pol beta) has been determined at 2.3 A resolution and refined to an R factor of 0.22. The mixed alpha/beta protein has three subdomains arranged in an overall U shape reminiscent of other polymerase structures. The folding topology of pol beta, however, is unique. Two divalent metals bind near three aspartic acid residues implicated in the catalytic activity. In the presence of Mn2+ and dTTP, interpretable electron density is seen for two metals and the triphosphate, but not the deoxythymidine moiety. The principal interaction of the triphosphate moiety is with the bound divalent metals.
About this Structure
1RPL is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
2.3 A crystal structure of the catalytic domain of DNA polymerase beta., Davies JF 2nd, Almassy RJ, Hostomska Z, Ferre RA, Hostomsky Z, Cell. 1994 Mar 25;76(6):1123-33. PMID:8137427
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