1t7p

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(New page: 200px<br /><applet load="1t7p" size="450" color="white" frame="true" align="right" spinBox="true" caption="1t7p, resolution 2.2&Aring;" /> '''T7 DNA POLYMERASE COM...)
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Revision as of 00:55, 21 November 2007

Image:1t7p.gif

1t7p, resolution 2.2Å

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T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN

Overview

DNA polymerases change their specificity for nucleotide substrates with, each catalytic cycle, while achieving error frequencies in the range of, 10(-5) to 10(-6). Here we present a 2.2 A crystal structure of the, replicative DNA polymerase from bacteriophage T7 complexed with a, primer-template and a nucleoside triphosphate in the polymerase active, site. The structure illustrates how nucleotides are selected in a, template-directed manner, and provides a structural basis for a, metal-assisted mechanism of phosphoryl transfer by a large group of, related polymerases.

About this Structure

1T7P is a Protein complex structure of sequences from Bacteriophage t7 and Escherichia coli with MG and DG3 as ligands. Active as DNA-directed DNA polymerase, with EC number 2.7.7.7 Full crystallographic information is available from OCA.

Reference

Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 A resolution., Doublie S, Tabor S, Long AM, Richardson CC, Ellenberger T, Nature. 1998 Jan 15;391(6664):251-8. PMID:9440688

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