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Human DEAD-box RNA-helicase DDX19 in complex with ADPHuman DEAD-box RNA-helicase DDX19 in complex with ADP
Structural highlights
FunctionDD19B_HUMAN ATP-dependent RNA helicase involved in mRNA export from the nucleus. Rather than unwinding RNA duplexes, DDX19B functions as a remodeler of ribonucleoprotein particles, whereby proteins bound to nuclear mRNA are dissociated and replaced by cytoplasmic mRNA binding proteins. Evolutionary Conservation![]() Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedDEXD/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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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OCA- Homo sapiens
- Large Structures
- Andersson j
- Arrowsmith ch
- Berglund h
- Bountra c
- Collins r
- Dahlgren lg
- Edwards am
- Flodin s
- Flores a
- Graslund s
- Hammarstrom m
- Johansson a
- Johansson i
- Karlberg t
- Kotenyova t
- Lehtio l
- Moche m
- Nilsson me
- Nordlund p
- Nyman t
- Olesen k
- Persson c
- Sagemark j
- Schueler h
- Thorsell ag
- Tresaugues l
- Van den berg s
- Weigelt j
- Welin m
- Wikstrom m
- Wisniewska m