1t7p | pdb_00001t7p
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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
Page seeded by OCA on Wed Nov 21 03:03:12 2007
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- Bacteriophage t7
- DNA-directed DNA polymerase
- Escherichia coli
- Protein complex
- Doublie, S.
- Ellenberger, T.
- Long, A.M.
- Richardson, C.C.
- Tabor, S.
- DG3
- MG
- Complex (hydrolase/electron transport/dna)
- Dna replication
- Nucleotidyl transferase
- Processivity factor
- Sequencing
- T7 dna polymerase
- Thioredoxin
