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

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 Klose (), Armen Y. Mulkidjanian (), Beat H. Meier () and Thomas Wiegand ()
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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
Anja Böckmann: Molecular Microbiology and Structural Biochemistry UMR 5086 CNRS/Université de Lyon
Daniel Klose: ETH Zürich
Armen Y. Mulkidjanian: Osnabrück University
Beat H. Meier: ETH Zürich
Thomas Wiegand: ETH Zürich

Nature Communications, 2021, vol. 12, issue 1, 1-13

Abstract: 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.

Date: 2021
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DOI: 10.1038/s41467-021-25599-z

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