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3EWS

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

Summary for 3EWS
Entry DOI10.2210/pdb3ews/pdb
DescriptorATP-dependent RNA helicase DDX19B, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
Functional Keywordsrna helicase, dead, adp, structural genomics, structural genomics consortium, sgc, rrna, atp-binding, hydrolase, nucleotide-binding, rna-binding, mrna, alternative splicing, cytoplasm, helicase, membrane, mrna transport, nuclear pore complex, nucleus, protein transport, translocation, transport
Biological sourceHomo sapiens (Human)
Cellular locationCytoplasm: Q9UMR2
Total number of polymer chains2
Total formula weight101848.22
Authors
Primary citationCollins, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.7 Å)
Structure validation

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