1t3n

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(New page: 200px<br /> <applet load="1t3n" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t3n, resolution 2.3&Aring;" /> '''Structure of the cat...)
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Revision as of 17:13, 12 November 2007

Image:1t3n.gif

1t3n, resolution 2.3Å

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Structure of the catalytic core of DNA polymerase Iota in complex with DNA and dTTP

Overview

Almost all DNA polymerases show a strong preference for incorporating the, nucleotide that forms the correct Watson-Crick base pair with the template, base. In addition, the catalytic efficiencies with which any given, polymerase forms the four possible correct base pairs are roughly the, same. Human DNA polymerase-iota (hPoliota), a member of the Y family of, DNA polymerases, is an exception to these rules. hPoliota incorporates the, correct nucleotide opposite a template adenine with a several hundred to, several thousand fold greater efficiency than it incorporates the correct, nucleotide opposite a template thymine, whereas its efficiency for correct, nucleotide incorporation opposite a template guanine or cytosine is, intermediate between these two extremes. Here we present the crystal, structure of hPoliota bound to a template primer and an incoming, nucleotide. The structure reveals a polymerase that is 'specialized' for, Hoogsteen base-pairing, whereby the templating base is driven to the syn, conformation. Hoogsteen base-pairing offers a basis for the varied, efficiencies and fidelities of hPoliota opposite different template bases, and it provides an elegant mechanism for promoting replication through, minor-groove purine adducts that interfere with replication.

About this Structure

1T3N is a Single protein structure of sequence from Homo sapiens with MG and TTP as ligands. Full crystallographic information is available from OCA.

Reference

Replication by human DNA polymerase-iota occurs by Hoogsteen base-pairing., Nair DT, Johnson RE, Prakash S, Prakash L, Aggarwal AK, Nature. 2004 Jul 15;430(6997):377-80. PMID:15254543

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