Journal
EMBO REPORTS
Volume 11, Issue 3, Pages 180-186Publisher
WILEY
DOI: 10.1038/embor.2010.11
Keywords
helicase; Prp43p; rRNA processing; splicing; X-ray crystallography
Categories
Funding
- Alfred Benzon Foundation
- Danish Science Research Council (FNU)
- Danish National Research Foundation
- Novo-Nordisk Foundation
- Div Of Molecular and Cellular Bioscience
- Direct For Biological Sciences [0743298] Funding Source: National Science Foundation
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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 carboxyterminal 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.
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