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Human DEAD-box RNA helicase DDX20, DEAD domain in complex with ADP

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PDB Code 2OXC Target Class DExD-DExH RNA helicases Target DDX20 Alias DDX20, DKFZp434H052, DP103, GEMIN3 Disease Area/Function neurobiology Date Deposited Feb 20 2007 Authors T.KARLBERG, D.OGG, C.H ARROWSMITH, H.BERGLUND, R.D.BUSAM, R.COLLINS, L.G.DAHLGREN, A.EDWARDS, S.FLODIN, A.FLORES, S.GRASLUND, B.M.HALLBERG, M.HAMMARSTROM, M.HOGBOM, I.JOHANSSON, T.KOTENYOVA, L.LEHTIO, M.MOCHE, P.NORDLUND, T.NYMAN, C.PERSSON, J.SAGEMARK, P.STENMARK, M.SUNDSTROM, A.G.THORSELL, S.VAN DENBERG, J.WEIGELT, L.HOLMBERG-SCHIAVONE, STRUCTURAL GENOMICSCONSORTIUM (SGC) Related Structure 3B7G

About this structure

The ATP-dependent DEAD-box RNA helicase 20 (EC 3.6.1.-, DDX20, DEAD box protein DP 103,Gemin-3) belongs to the RNA-binding DExD-box family of helicases that are involved in all aspects of cellular RNA-metabolism such as transcription, splicing, RNA nucleocytoplasmatic transport, translation and ribosome biogenesis. All proteins in this family are believed to bind and hydrolyze ATP using the energy to assist in the folding or unfolding of RNA or in the assembly/disassembly of RNA-protein complexes. Members of the family normally consist of two conserved domains which contain 9 signature motives that are involved in ATP-binding and hydrolysis, substrate binding and helicase activity (Cordin et al. 2006). Additional domains that are unique to a particular helicase usually flank the two conserved domains.

DDX20 was initially identified as a protein that associates with Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C that regulate transcription of several genes (Grundhoff et al. 1999). Recent results suggest that DDX20 itself is a transcriptional regulator and it is speculated that the protein represses transcription through recruitment of histone deacetylases (Fuller-Pace, 2006). DDX20 is also suggested to be involved in snRNP assembly (Charroux et al. 1999). Conserved domain 1 of DDX20, containing the signature DEAD-box motif was crystallized in the presence of ADP and the three-dimensional structure determined at 1.3 Å. The structure shows that domain 1 of the protein folds into an α-β RecA-like domain with ADP clearly visible in the nucleotide-binding site.

We have also solved the Human DEAD-box RNA helicase DDX20, conserved domain I in complex with AMPPNP (PDB 3B7G).

References

  1. Cordin O., Banroques J., Tanner N.K., and Linder P. (2005) The DEAD-box protein family of RNA helicases. Gene 367: 17-37. PubMed 16337753
  2. Fuller-Pace F.P. (2006) DExD/H box RNA helicases: multifunctional proteins with important roles in transcriptional regulation. Nucleic Acids Res. 34:4206-15. PubMed 16935882
  3. Grundhoff A.T., Kremmer E., Tureci O., Glieden A., Gindorf C., Atz J., Mueller-Lantzsch N., Schubach W.H. and Grasser F.A. (1999) Characterization of DP103, a novel DEAD box protein that binds to the Epstein-Barr virus nuclear proteins EBNA2 and EBNA3C. J. Biol. Chem. 274:19136-44. PubMed 10383418
  4. Charroux B., Pellizzoni L., Perkinson R.A., Shevchenko A., Mann M. and Dreyfuss G. (1999) Gemin3: A novel DEAD box protein that interacts with SMN, the spinal muscular atrophy gene product, and is a component of gems. J. Cell Biol., 147:1181-1194. PubMed 10601333