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1t7p

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{{STRUCTURE_1t7p| PDB=1t7p | SCENE= }}
{{STRUCTURE_1t7p| PDB=1t7p | SCENE= }}
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'''T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN'''
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===T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_9440688}}
==About this Structure==
==About this Structure==
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[[Category: T7 dna polymerase]]
[[Category: T7 dna polymerase]]
[[Category: Thioredoxin]]
[[Category: Thioredoxin]]
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Revision as of 06:15, 29 July 2008

Image:1t7p.png

Template:STRUCTURE 1t7p

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

Template:ABSTRACT PUBMED 9440688

About this Structure

1T7P is a Protein complex structure of sequences from Enterobacteria phage t7 and Escherichia coli. 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

Page seeded by OCA on Tue Jul 29 09:15:33 2008

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