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Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution

Author

Listed:
  • Sylvie Doublié

    (Harvard Medical School)

  • Stanley Tabor

    (Harvard Medical School)

  • Alexander M. Long

    (Harvard Medical School)

  • Charles C. Richardson

    (Harvard Medical School)

  • Tom Ellenberger

    (Harvard Medical School)

Abstract

DNA polymerases change their specificity for nucleotide substrates with each catalytic cycle, while achieving error frequencies in the range of 10−5to 10−6. Here we present a 2.2 Å 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.

Suggested Citation

  • Sylvie Doublié & Stanley Tabor & Alexander M. Long & Charles C. Richardson & Tom Ellenberger, 1998. "Crystal structure of a bacteriophage T7 DNA replication complex at 2.2 Å resolution," Nature, Nature, vol. 391(6664), pages 251-258, January.
    • Handle: RePEc:nat:nature:v:391:y:1998:i:6664:d:10.1038_34593
    DOI: 10.1038/34593
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    Cited by:

    1. Ju-Sim Kim & Alexandra Born & James Karl A. Till & Lin Liu & Sashi Kant & Morkos A. Henen & Beat Vögeli & Andrés Vázquez-Torres, 2022. "Promiscuity of response regulators for thioredoxin steers bacterial virulence," Nature Communications, Nature, vol. 13(1), pages 1-15, December.
    2. Longfu Xu & Matthew T. J. Halma & Gijs J. L. Wuite, 2024. "Mapping fast DNA polymerase exchange during replication," Nature Communications, Nature, vol. 15(1), pages 1-11, December.
    3. Gina Buchel & Ashok R. Nayak & Karl Herbine & Azadeh Sarfallah & Viktoriia O. Sokolova & Angelica Zamudio-Ochoa & Dmitry Temiakov, 2023. "Structural basis for DNA proofreading," Nature Communications, Nature, vol. 14(1), pages 1-12, December.

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