Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases-Reference-Cited by-同舟云学术

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Structures of phi29 DNA polymerase complexed with substrate: the mechanism of translocation in B-family polymerases

Published:2007-07-05 Issue:14 Volume:26 Page:3494-3505
ISSN:0261-4189
Container-title:The EMBO Journal
language:
Short-container-title:EMBO J

Author:

Berman Andrea J,Kamtekar Satwik,Goodman Jessica L,Lázaro José M,de Vega Miguel,Blanco Luis,Salas Margarita,Steitz Thomas A

Publisher

Wiley

Subject

General Immunology and Microbiology,General Biochemistry, Genetics and Molecular Biology,Molecular Biology,General Neuroscience

Reference55 articles.

1. A single side chain prevents Escherichia coli DNA polymerase I (Klenow fragment) from incorporating ribonucleotides

2. Crystal structures of the Klenow fragment of DNA polymerase I complexed with deoxynucleoside triphosphate and pyrophosphate

3. Relating Structure to Function in 29 DNA Polymerase

4. Phi 29 DNA polymerase active site. Mutants in conserved residues Tyr254 and Tyr390 are affected in dNTP binding.

5. Phi 29 DNA polymerase active site. The conserved amino acid motif “Kx3NSxYG” is involved in template-primer binding and dNTP selection

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