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.
