학술논문
Spectroscopic glimpses of the transition state of ATP hydrolysis trapped in a bacterial DnaB helicase.
Document Type
Academic Journal
Author
Malär AA; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Wili N; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Völker LA; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Kozlova MI; Department of Physics, Osnabrück University, Osnabrück, Germany.; Cadalbert R; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Däpp A; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Weber ME; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Zehnder J; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Jeschke G; Physical Chemistry, ETH Zürich, Zürich, Switzerland.; Eckert H; Institut für Physikalische Chemie, WWU Münster, Münster, Germany.; Instituto de Física de Sao Carlos, Universidade de Sao Paulo, Sao Carlos, SP, Brazil.; Böckmann A; Molecular Microbiology and Structural Biochemistry UMR 5086 CNRS/Université de Lyon, Lyon, France.; Klose D; Physical Chemistry, ETH Zürich, Zürich, Switzerland. daniel.klose@phys.chem.ethz.ch.; Mulkidjanian AY; Department of Physics, Osnabrück University, Osnabrück, Germany. armen.mulkidjanian@uni-osnabrueck.de.; School of Bioengineering and Bioinformatics and Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State University, Moscow, Russia. armen.mulkidjanian@uni-osnabrueck.de.; Meier BH; Physical Chemistry, ETH Zürich, Zürich, Switzerland. beme@ethz.ch.; Wiegand T; Physical Chemistry, ETH Zürich, Zürich, Switzerland. thomas.wiegand@phys.chem.ethz.ch.; Max-Planck-Institute for Chemical Energy Conversion, Mülheim an der Ruhr, Germany. thomas.wiegand@phys.chem.ethz.ch.; Institute of Technical and Macromolecular Chemistry, RWTH Aachen, Aachen, Germany. thomas.wiegand@phys.chem.ethz.ch.
Source
Publisher: Nature Pub. Group Country of Publication: England NLM ID: 101528555 Publication Model: Electronic Cited Medium: Internet ISSN: 2041-1723 (Electronic) Linking ISSN: 20411723 NLM ISO Abbreviation: Nat Commun Subsets: MEDLINE
Subject
Language
English
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 31 P, 1 H 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. 19 F and 27 Al 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.
(© 2021. The Author(s).)
(© 2021. The Author(s).)