3ews

Human DEAD-box RNA-helicase DDX19 in complex with ADPHuman DEAD-box RNA-helicase DDX19 in complex with ADP

Publication Abstract from PubMed

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DEXD/H-box RNA helicases couple ATP hydrolysis to RNA remodeling by an unknown mechanism. We used x-ray crystallography and biochemical analysis of the human DEXD/H-box protein DDX19 to investigate its regulatory mechanism. The crystal structures of DDX19, in its RNA-bound prehydrolysis and free posthydrolysis state, reveal an alpha-helix that inserts between the conserved domains of the free protein to negatively regulate ATPase activity. This finding was corroborated by biochemical data that confirm an autoregulatory function of the N-terminal region of the protein. This is the first study describing crystal structures of a DEXD/H-box protein in its open and closed cleft conformations.

The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch., Collins R, Karlberg T, Lehtio L, Schutz P, van den Berg S, Dahlgren LG, Hammarstrom M, Weigelt J, Schuler H, J Biol Chem. 2009 Apr 17;284(16):10296-300. Epub 2009 Feb 25. PMID:19244245

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this StructureAbout this Structure

3ews is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See AlsoSee Also

• DEAD-box RNA-helicase DDX19 in complex with ADP
• Dead-box RNA helicase DDX19%2C in complex with an ATP-analogue and RNA
• Helicase