Ontology highlight
ABSTRACT:
SUBMITTER: Manthei KA
PROVIDER: S-EPMC4394303 | biostudies-literature | 2015 Apr
REPOSITORIES: biostudies-literature
Manthei Kelly A KA Hill Morgan C MC Burke Jordan E JE Butcher Samuel E SE Keck James L JL
Proceedings of the National Academy of Sciences of the United States of America 20150323 14
RecQ helicases unwind remarkably diverse DNA structures as key components of many cellular processes. How RecQ enzymes accommodate different substrates in a unified mechanism that couples ATP hydrolysis to DNA unwinding is unknown. Here, the X-ray crystal structure of the Cronobacter sakazakii RecQ catalytic core domain bound to duplex DNA with a 3' single-stranded extension identifies two DNA-dependent conformational rearrangements: a winged-helix domain pivots ∼90° to close onto duplex DNA, an ...[more]