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Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase

Author

Listed:
  • Alexander A. Malär

    (ETH Zürich)

  • Nino Wili

    (ETH Zürich)

  • Laura A. Völker

    (ETH Zürich)

  • Maria I. Kozlova

    (Osnabrück University)

  • Riccardo Cadalbert

    (ETH Zürich)

  • Alexander Däpp

    (ETH Zürich)

  • Marco E. Weber

    (ETH Zürich)

  • Johannes Zehnder

    (ETH Zürich)

  • Gunnar Jeschke

    (ETH Zürich)

  • Hellmut Eckert

    (WWU Münster
    Universidade de Sao Paulo)

  • Anja Böckmann

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

  • Daniel Klose

    (ETH Zürich)

  • Armen Y. Mulkidjanian

    (Osnabrück University
    Lomonosov Moscow State University)

  • Beat H. Meier

    (ETH Zürich)

  • Thomas Wiegand

    (ETH Zürich
    Max-Planck-Institute for Chemical Energy Conversion
    RWTH Aachen)

Abstract

The ATP hydrolysis transition state of motor proteins is a weakly populated protein state that can be stabilized and investigated by replacing ATP with chemical mimics. We present atomic-level structural and dynamic insights on a state created by ADP aluminum fluoride binding to the bacterial DnaB helicase from Helicobacter pylori. We determined the positioning of the metal ion cofactor within the active site using electron paramagnetic resonance, and identified the protein protons coordinating to the phosphate groups of ADP and DNA using proton-detected 31P,1H solid-state nuclear magnetic resonance spectroscopy at fast magic-angle spinning > 100 kHz, as well as temperature-dependent proton chemical-shift values to prove their engagements in hydrogen bonds. 19F and 27Al MAS NMR spectra reveal a highly mobile, fast-rotating aluminum fluoride unit pointing to the capture of a late ATP hydrolysis transition state in which the phosphoryl unit is already detached from the arginine and lysine fingers.

Suggested Citation

  • Alexander A. Malär & Nino Wili & Laura A. Völker & Maria I. Kozlova & Riccardo Cadalbert & Alexander Däpp & Marco E. Weber & Johannes Zehnder & Gunnar Jeschke & Hellmut Eckert & Anja Böckmann & Daniel, 2021. "Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase," Nature Communications, Nature, vol. 12(1), pages 1-13, December.
    • Handle: RePEc:nat:natcom:v:12:y:2021:i:1:d:10.1038_s41467-021-25599-z
    DOI: 10.1038/s41467-021-25599-z
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