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3g0h

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

Publication Abstract from PubMed

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 Structure

3g0h, resolution 2.70Å ()
Sites: , and
Ligands: , ,
Gene: DBP5, DDX19, DDX19B (Homo sapiens)
Related: 3ews
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml


3G0H is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

bound. .

DDX19 is .

  • With RNA and the ATP analog bound, the N-terminal extension (dark green) is tucked at the side and the two domains are close together.
  • This conformation is presumed to resemble the pre-hydrolysis state in which RNA is bound. It is also referred to as the closed state and closed cleft conformation.
  • This scene is similar to the view in Figure 1C of the paper describing the structure.

Showing is bound.

  • This overlay clearly illustrates the dramatic shift in the location of the N-terminal extension (dark green).
  • This view clearly shows how the N-terminal helix of the extension extends from the RNA-binding site to down near the ATP-binding site.

. The placement of the N-terminal extension between the two helicase domains negatively regulates ATPase activity. A .

  • Of particular note is arginine 429, the so-called arginine finger, that is essential for ATPase activity. for ATPase function.
  • illustrates how it is moved away from the active site when RNA is not bound and hydrolysis has occurred to produce ADP.
  • Keep in mind the intermediate models, in between the endpoints, are hypothetical.

See also

3ews is human DDX19 with ADP bound. It is used in the morphs here and was described in the same article as 3g0h.

Reference

  • Collins R, Karlberg T, Lehtio L, Schutz P, van den Berg S, Dahlgren LG, Hammarstrom M, Weigelt J, Schuler H. The DEXD/H-box RNA helicase DDX19 is regulated by an {alpha}-helical switch. J Biol Chem. 2009 Apr 17;284(16):10296-300. Epub 2009 Feb 25. PMID:19244245 doi:10.1074/jbc.C900018200

Page originally seeded by OCA on Wed Apr 29 20:54:05 2009

Proteopedia Page Contributors and Editors (what is this?)

Wayne Decatur, OCA

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