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Citation
Tags
HERO ID
7768103
Reference Type
Journal Article
Subtype
Review
Title
ATP Analogues for Structural Investigations: Case Studies of a DnaB Helicase and an ABC Transporter
Author(s)
Lacabanne, D; Wiegand, T; Wili, N; Kozlova, MI; Cadalbert, R; Klose, D; Mulkidjanian, AY; Meier, BH; Böckmann, A
Year
2020
Is Peer Reviewed?
1
Journal
Molecules
ISSN:
1420-3049
Volume
25
Issue
22
Language
English
PMID
33198135
DOI
10.3390/molecules25225268
Web of Science Id
WOS:000594228000001
Abstract
Nucleoside triphosphates (NTPs) are used as chemical energy source in a variety of cell systems. Structural snapshots along the NTP hydrolysis reaction coordinate are typically obtained by adding stable, nonhydrolyzable adenosine triphosphate (ATP) -analogues to the proteins, with the goal to arrest a state that mimics as closely as possible a physiologically relevant state, e.g., the pre-hydrolytic, transition and post-hydrolytic states. We here present the lessons learned on two distinct ATPases on the best use and unexpected pitfalls observed for different analogues. The proteins investigated are the bacterial DnaB helicase from Helicobacter pylori and the multidrug ATP binding cassette (ABC) transporter BmrA from Bacillus subtilis, both belonging to the same division of P-loop fold NTPases. We review the magnetic-resonance strategies which can be of use to probe the binding of the ATP-mimics, and present carbon-13, phosphorus-31, and vanadium-51 solid-state nuclear magnetic resonance (NMR) spectra of the proteins or the bound molecules to unravel conformational and dynamic changes upon binding of the ATP-mimics. Electron paramagnetic resonance (EPR), and in particular W-band electron-electron double resonance (ELDOR)-detected NMR, is of complementary use to assess binding of vanadate. We discuss which analogues best mimic the different hydrolysis states for the DnaB helicase and the ABC transporter BmrA. These might be relevant also to structural and functional studies of other NTPases.
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Vanadium Compounds - Problem Formulation
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