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EMBO Rep. 2010 Mar;11(3):180-6. doi: 10.1038/embor.2010.11. Epub 2010 Feb 19.

Structural basis for the function of DEAH helicases.

Author information

1
Department of Molecular Biology, Aarhus University, Aarhus, Denmark.

Abstract

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 hairpin that are important for RNA unwinding or ribonucleoprotein remodelling. The structure of Prp43p provides the framework for functional and genetic analysis of all DEAH helicases.

PMID:
20168331
PMCID:
PMC2838688
DOI:
10.1038/embor.2010.11
[Indexed for MEDLINE]
Free PMC Article

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