1t7p
From Proteopedia
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'''T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN''' | '''T7 DNA POLYMERASE COMPLEXED TO DNA PRIMER/TEMPLATE,A NUCLEOSIDE TRIPHOSPHATE, AND ITS PROCESSIVITY FACTOR THIOREDOXIN''' | ||
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[[Category: Richardson, C C.]] | [[Category: Richardson, C C.]] | ||
[[Category: Tabor, S.]] | [[Category: Tabor, S.]] | ||
- | [[Category: | + | [[Category: Dna replication]] |
- | + | [[Category: Nucleotidyl transferase]] | |
- | [[Category: | + | [[Category: Processivity factor]] |
- | [[Category: | + | [[Category: Sequencing]] |
- | [[Category: | + | [[Category: T7 dna polymerase]] |
- | [[Category: | + | [[Category: Thioredoxin]] |
- | [[Category: | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:38:21 2008'' |
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Revision as of 06:38, 3 May 2008
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 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 Sat May 3 09:38:21 2008