Structural basis for the function of DEAH helicases.

@article{He2010StructuralBF,
  title={Structural basis for the function of DEAH helicases.},
  author={Yangzi He and Gregers Rom Andersen and Klaus Hvid Nielsen},
  journal={EMBO reports},
  year={2010},
  volume={11 3},
  pages={180-6}
}
DEAH helicases participate in pre-messenger RNA splicing and ribosome biogenesis. The structure of yeast Prp43p-ADP reveals the homology of DEAH helicases to DNA helicases and the presence of an oligonucleotide-binding motif. A beta-hairpin from the second RecA domain is wedged between two carboxy-terminal domains and blocks access to the occluded RNA binding site formed by the RecA domains and a C-terminal domain. ATP binding and hydrolysis are likely to induce conformational changes in the… CONTINUE READING