3G0H

Human dead-box RNA helicase DDX19, in complex with an ATP-analogue and RNA

Summary for 3G0H

• Entry DOI: 10.2210/pdb3g0h/pdb
• Related: 3EWS
• Descriptor: ATP-dependent RNA helicase DDX19B, 5'-R(P*UP*UP*UP*UP*UP*UP*U)-3', PHOSPHOAMINOPHOSPHONIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: protein-rna complex, dbp5, structural genomics, structural genomics consortium, sgc, atp-binding, helicase, hydrolase, membrane, mrna transport, nuclear pore complex, nucleotide-binding, nucleus, phosphoprotein, protein transport, rna-binding, translocation, transport, polyuracil, hydrolase-rna complex, hydrolase/rna
• Biological source: Homo sapiens (Human)
• Cellular location: Cytoplasm: Q9UMR2
• Total number of polymer chains: 2
• Total formula weight: 50746.04

Authors

Karlberg, T.,Lehtio, L.,Collins, R.,Arrowsmith, C.H.,Berglund, H.,Bountra, C.,Dahlgren, L.G.,Edwards, A.M.,Flodin, S.,Flores, A.,Graslund, S.,Hammarstrom, M.,Johansson, A.,Johansson, I.,Kotenyova, T.,Moche, M.,Nilsson, M.E.,Nordlund, P.,Nyman, T.,Persson, C.,Sagemark, J.,Schutz, P.,Siponen, M.I.,Thorsell, A.G.,Tresaugues, L.,Van Den Berg, S.,Weigelt, J.,Welin, M.,Wisniewska, M.,Schuler, H.,Structural Genomics Consortium (SGC) (deposition date: 2009-01-28, release date: 2009-02-17, Last modification date: 2023-09-06)

Primary citation

Collins, R.,Karlberg, T.,Lehtio, L.,Schutz, P.,van den Berg, S.,Dahlgren, L.G.,Hammarstrom, M.,Weigelt, J.,Schuler, H.
The DEXD/H-box RNA Helicase DDX19 Is Regulated by an {alpha}-Helical Switch.
J.Biol.Chem., 284:10296-10300, 2009

PubMed Abstract: 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.

PubMed: 19244245
DOI: 10.1074/jbc.C900018200

Experimental method

X-RAY DIFFRACTION (2.7 Å)