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- Title
The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase.
- Authors
Wiegand, Thomas; Cadalbert, Riccardo; Lacabanne, Denis; Timmins, Joanna; Terradot, Laurent; Böckmann, Anja; Meier, Beat H.
- 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. DnaB helicases are motor proteins that couple ATP-hydrolysis to the movement of the protein along single-stranded DNA leading to a separation of double-stranded DNA at the replication fork. Here authors use solid-state NMR spectroscopy and reveal DnaB's conformational responses to ATP hydrolysis and the resulting DNA loading and translocation.
- Publication
Nature Communications, 2019, Vol 10, Issue 1, p1
- ISSN
2041-1723
- Publication type
Article
- DOI
10.1038/s41467-018-07968-3