The conformational changes coupling ATP hydrolysis and translocation in a bacterial DnaB helicase.

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 t

SUBMITTER: Wiegand T 

PROVIDER: S-EPMC6318325 | biostudies-literature | 2019 Jan

REPOSITORIES: biostudies-literature