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The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase

Author

Listed:
  • Thomas Wiegand

    (Physical Chemistry, ETH Zurich)

  • Riccardo Cadalbert

    (Physical Chemistry, ETH Zurich)

  • Denis Lacabanne

    (Physical Chemistry, ETH Zurich
    Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS/Université de Lyon)

  • Joanna Timmins

    (Univ. Grenoble Alpes, CNRS, CEA, CNRS, IBS)

  • Laurent Terradot

    (Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS/Université de Lyon)

  • Anja Böckmann

    (Molecular Microbiology and Structural Biochemistry, Labex Ecofect, UMR 5086 CNRS/Université de Lyon)

  • Beat H. Meier

    (Physical Chemistry, ETH Zurich)

Abstract

DnaB helicases are motor proteins that couple ATP-hydrolysis to the loading of the protein onto DNA at the replication fork and to translocation along DNA to separate double-stranded DNA into single strands during replication. Using a network of conformational states, arrested by nucleotide mimics, we herein characterize the reaction coordinates for ATP hydrolysis, DNA loading and DNA translocation using solid-state NMR spectroscopy. AMP-PCP is used as pre-hydrolytic, ADP:AlF4− as transition state, and ADP as post-hydrolytic ATP mimic. 31P and 13C NMR spectra reveal conformational and dynamic responses to ATP hydrolysis and the resulting DNA loading and translocation with single amino-acid resolution. This allows us to identify residues guiding the DNA translocation process and to explain the high binding affinities for DNA observed for ADP:AlF4−, which turns out to be optimally preconfigured to bind DNA.

Suggested Citation

  • Thomas Wiegand & Riccardo Cadalbert & Denis Lacabanne & Joanna Timmins & Laurent Terradot & Anja Böckmann & Beat H. Meier, 2019. "The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase," Nature Communications, Nature, vol. 10(1), pages 1-11, December.
    • Handle: RePEc:nat:natcom:v:10:y:2019:i:1:d:10.1038_s41467-018-07968-3
    DOI: 10.1038/s41467-018-07968-3
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    Cited by:

    1. Lauriane Lecoq & Louis Brigandat & Rebecca Huber & Marie-Laure Fogeron & Shishan Wang & Marie Dujardin & Mathilde Briday & Thomas Wiegand & Morgane Callon & Alexander Malär & David Durantel & Dara Bur, 2023. "Molecular elucidation of drug-induced abnormal assemblies of the hepatitis B virus capsid protein by solid-state NMR," Nature Communications, Nature, vol. 14(1), pages 1-14, December.

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