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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.

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Categories: Homo sapiens | Arrowsmith, C H. | Berg, S Van Den. | Berglund, H. | Bountra, C. | Collins, R. | Dahlgren, L G. | Edwards, A M. | Flodin, S. | Flores, A. | Graslund, S. | Hammarstrom, M. | Johansson, A. | Johansson, I. | Karlberg, T. | Kotenyova, T. | Lehtio, L. | Moche, M. | Nilsson, M E. | Nordlund, P. | Nyman, T. | Persson, C. | SGC, Structural Genomics Consortium. | Sagemark, J. | Schuler, H. | Schutz, P. | Siponen, M I. | Thorsell, A G. | Tresaugues, L. | Weigelt, J. | Welin, M. | Wisniewska, M. | Atp-binding | Dbp5 | Helicase | Hydrolase | Hydrolase-rna complex | Membrane | Mrna transport | Nuclear pore complex | Nucleotide-binding | Nucleus | Phosphoprotein | Polyuracil | Protein transport | Protein-rna complex | Rna-binding | Sgc | Structural genomic | Structural genomics consortium | Translocation | Transport