2fmp: Difference between revisions

Revision as of 07:08, 29 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:2fmp.png

Template:STRUCTURE 2fmp

DNA Polymerase beta with a terminated gapped DNA substrate and ddCTP with sodium in the catalytic siteDNA Polymerase beta with a terminated gapped DNA substrate and ddCTP with sodium in the catalytic site

Template:ABSTRACT PUBMED 16615916

About this StructureAbout this Structure

2FMP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Magnesium-induced assembly of a complete DNA polymerase catalytic complex., Batra VK, Beard WA, Shock DD, Krahn JM, Pedersen LC, Wilson SH, Structure. 2006 Apr;14(4):757-66. PMID:16615916

Page seeded by OCA on Tue Jul 29 07:08:05 2008

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OCA

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-'''DNA Polymerase beta with a terminated gapped DNA substrate and ddCTP with sodium in the catalytic site'''
+===DNA Polymerase beta with a terminated gapped DNA substrate and ddCTP with sodium in the catalytic site===
-==Overview==
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-The molecular details of the nucleotidyl transferase reaction have remained speculative, as strategies to trap catalytic intermediates for structure determination utilize substrates lacking the primer terminus 3'-OH and catalytic Mg2+, resulting in an incomplete and distorted active site geometry. Since the geometric arrangement of these essential atoms will impact chemistry, structural insight into fidelity strategies has been hampered. Here, we present a crystal structure of a precatalytic complex of a DNA polymerase with bound substrates that include the primer 3'-OH and catalytic Mg2+. This catalytic intermediate was trapped with a nonhydrolyzable deoxynucleotide analog. Comparison with two new structures of DNA polymerase beta lacking the 3'-OH or catalytic Mg2+ is described. These structures provide direct evidence that both atoms are required to achieve a proper geometry necessary for an in-line nucleophilic attack of O3' on the alphaP of the incoming nucleotide.
+The line below this paragraph, {{ABSTRACT_PUBMED_16615916}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16615916 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_16615916}}
 ==About this Structure==
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 [[Category: Wilson, S H.]]
 [[Category: Nucleotidyl transferase]]
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