Please contact us for any questions or request for reagents for this structure.

Human DEAD box RNA helicase DDX5 (p68)

Click on the iSee icon to launch an enhanced annotation with interactive 3D representations and animated transitions. Please note that a web plugin (activeICM) is required to access this enhanced functionality. Instructions for the installation and use of the web plugin are available.

PDB Code 3FE2 Target Class ATPases Target DDX5 Alias DDX5, DKFZp686J01190, G17P1, HLR1, HUMP68, p68 Disease Area/Function cancer Date Deposited Nov 27 2008 Authors T.KARLBERG, M.I.SIPONEN, C.H.ARROWSMITH, H.BERGLUND, C.BOUNTRA, R.COLLINS, L.G.DAHLGREN, A.M.EDWARDS, S.FLODIN, A.FLORES, S.GRASLUND, M.HAMMARSTROM, A.JOHANSSON, I.JOHANSSON, T.KOTENYOVA, L.LEHTIO, M.MOCHE, M.E.NILSSON, P.NORDLUND, T.NYMAN, C.PERSSON, J.SAGEMARK, A.G.THORSELL, L.TRESAUGUES, S.VAN DEN BERG, J.WEIGELT, M.WELIN, M.WIKSTROM, M.WISNIEWSKA, H.SCHULER

About this structure

DDX5 (EC=3.6.1.- DEAD box protein 5, RNA helicase p68) belongs to the ATP-dependent DEAD box subfamily of RNA helicases that is characterized by the presence of several conserved motifs, including the signature DEAD sequence. The DEAD box RNA helicases play important roles in all aspects of cellular RNA metabolism e.g. pre-mRNA splicing, transcription, ribosome biogenesis, export, translation (Cordin et al. 2005). DDX5 shares 90% protein sequence similarity with DDX17 (p72) in the central core, but the N- and C-terminal extensions are significantly different. DDX5 and DDX17 have been suggested to exist as heterodimers in a variety of complexes in the cell. (Ogilvie et al 2003). Both proteins act as transcriptional co-activators; this has been shown for the activation of transcription of ERα (Endoh et al. 1999), MyoD (Caretti et al 2006) and p53 tumor suppressor (Bates et al 2005). DDX5 and DDX17 may be important for the recruitment of specific components of the transcription machinery, including chromatin remodeling factors, and they may facilitate formation and stabilization of the initiation complex (Caretti et al. 2007).

The structure of the DEAD domain of DDX5 was solved and refined to 2.6 Å resolution. It shows the typical DEAD domain structure, with a central 8-stranded β-sheet sandwiched between 5 α-helices on each face, and one ADP molecule in the nucleotide binding pocket.

References

  1. Cordin O., Banroques N., Kyle Tanner N., Linder P. (2005) The DEAD-box protein family of RNA helicases. Gene 367: 17-37.
  2. Ogilvie V.C., Wilson B.J., Nicol S.M., Morrice N.A., Saunders L.R., Barber G.N. and Fuller-Pace F.V. (2003) The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells. Nucleic Acids Res 31:1470-1480.
  3. Endoh H., Maruyama K., Masuhiro Y., Kobayashi Y., Goto M., Tai H., Yanagisawa J., Metzger D., Hashimoto S. and Kato S. Purification and identification of p68 RNA helicase acting as a transcriptional coactivator specific for the activation function 1 of human estrogen receptor α. Mol. Cell. Biol. 19:5363-5372.
  4. Bates G. J., Nicol S.M., Wilson B.J., Jacobs A.M., Bourdon J.C., Wardrop J., Gregory D:J:, Lane D:P:, Perkins N.D. and Fuller-Pace F.V. (2005) The DEAD box protein p68: a novel transcriptional coactivator of the p53 tumour suppressor. EMBO J. 24:243-253.
  5. Caretti G., Schiltz R.L., Dilworth F.J., DiPadova M., Zhao P., Ogryzko V., Fuller-Pace F.V., Hoffman E.P., Tapscott S.J. and Sartorelli V. (2006) The RNA helicases p68/p72 and the noncoding RNA SRA are coregulaters of MyoD and skeletal muscle differentiation. Dev. Cell 11:547-560.
  6. Caretti G., Lei E.P. and Sartorelli V. (2007) The DEAD-box p68/p72 proteins and the noncoding RNA steroid receptor activator SRA: eclectic regulators of disparate biological functions. Cell Cycle 6:1172-1176.