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Open AccessReview

Structural Basis of DEAH/RHA Helicase Activity

Biochemistry and Biophysics Center, National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA
Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK
Author to whom correspondence should be addressed.
Academic Editor: Jinwei Zhang
Crystals 2017, 7(8), 253;
Received: 6 July 2017 / Revised: 12 August 2017 / Accepted: 13 August 2017 / Published: 15 August 2017
(This article belongs to the Special Issue Nucleic Acid Crystallography)
PDF [21528 KB, uploaded 16 August 2017]


DEAH/RHA helicases are members of a large group of proteins collectively termed DExH-box, which also include Ski2-like and NS3/NPH-II helicases. By binding and remodeling DNA and RNA, DEAH/RHA helicases play critical roles in many cellular processes ranging from transcription and splicing to ribosome biogenesis, innate immunity and stress granule formation. While numerous crystal structures of other DExH-box proteins helicases have been reported, no structures of DEAH/RHA helicases bound to nucleic acid substrates have been available until the recent co-crystal structures of the maleless (MLE) and Prp43p bound to RNA. This review examines how these new structures provide a starting point to understand how DEAH/RHA helicases bind to, translocate on, and unwind nucleic acid substrates. View Full-Text
Keywords: DEAH/RHA; DExH; helicase; MLE; Prp43p; DHX36; HCV NS3 DEAH/RHA; DExH; helicase; MLE; Prp43p; DHX36; HCV NS3

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Chen, M.C.; Ferré-D’Amaré, A.R. Structural Basis of DEAH/RHA Helicase Activity. Crystals 2017, 7, 253.

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