1rpl

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{{STRUCTURE_1rpl| PDB=1rpl | SCENE= }}
{{STRUCTURE_1rpl| PDB=1rpl | SCENE= }}
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'''2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA'''
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===2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA===
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==Overview==
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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.
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(as it appears on PubMed at http://www.pubmed.gov), where 8137427 is the PubMed ID number.
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{{ABSTRACT_PUBMED_8137427}}
==About this Structure==
==About this Structure==
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[[Category: II, J F.Davies.]]
[[Category: II, J F.Davies.]]
[[Category: Nucleotidyltransferase]]
[[Category: Nucleotidyltransferase]]
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Revision as of 13:10, 29 July 2008

Image:1rpl.png

Template:STRUCTURE 1rpl

2.3 ANGSTROMS CRYSTAL STRUCTURE OF THE CATALYTIC DOMAIN OF DNA POLYMERASE BETA

Template:ABSTRACT PUBMED 8137427

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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