Structure of Taq polymerase with DNA at the polymerase active site
Article Abstract:
The blunt end of duplex DNA binds to the polymerase active-site cleft of the Taq polymerase, a Thermus aquaticus DNA polymerase. The structure of the bound DNA is similar to both A- and B-form DNAs. The DNA shows no bending or passing through the polymerase cleft. Highly conserved Taq amino acids are in contact with the bound DNA. The Taq side chains form hydrogen bonds with the DNA purines and pyrimidines. The DNA bound to the polymerase active site and the exonuclease site bind to the same region. However, they are translated relative to each other and have different interactions with Taq.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1996
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A mechanism for all polymerases
Article Abstract:
Replicative DNA polymerases are extremely processive, able to traverse the entire genome of a virus DNA without falling off. Doublie and colleagues and Kiefer and colleagues have provided insights into the processivity, fidelity and catalytic mechanism of DNA polymerases. Doublie and colleagues have captured the replicating DNA polymerase of bacteriophage T7 DNA, together with Escherichia coli thioredoxin. Kiefer and colleagues have shown the fidelity with which polymerases copy DNA in the co-crystal structure of Bacillus stearothermophilus.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1998
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Crystal structure of Thermus aquaticus DNA polymerase
Article Abstract:
Thermus aquaticus DNA polymerase is a homolog of Escherichia coli DNA polymerase and so its crystal structure was examined in the hopes of clarifying the polymerase chain reaction mechanism. However, though the use of phosphoryl transfer was documented, the structure raised as many questions as it solved. The questions were largely caused by the over 70 Angstrom distance between the polymerase and 5'-nuclease active sites that must cooperate in the fabrication of a nick-containing duplex DNA product.
Publication Name: Nature
Subject: Zoology and wildlife conservation
ISSN: 0028-0836
Year: 1995
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