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Human DEAD-box RNA-helicase DDX52, conserved domain I in complex with ADP

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PDB Code 3DKP Target Class ATPases Target DDX52 Alias DDX52, ROK1 Disease Area/Function cancer Date Deposited Jun 25 2008 Authors LEHTIO, L., KARLBERG, T., ANDERSSON, J., ARROWSMITH, C.H., BERGLUND, H., COLLINS, R., 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., OLESEN, K., PERSSON, C., SAGEMARK, J., THORSELL, A.G., TRESAUGUES, L., VAN DEN BERG, S., WELIN, M., WISNIEWSKA, M., WIKSTROM, M., SCHUELER, H.

About this structure

DDX52 (DEAD box protein 52, EC: 3.6.1.-) belongs to the ROK1 subfamily of DEAD-box proteins (1). DEAD-box proteins are also called RNA-helicases as they unwind double stranded RNA molecules in an ATP dependent manner. DDX52 is a nucleolar protein and it has high sequence similarity to the well-characterized Rok1p RNA of yeast. Rok1p is suggested to be involved in maturation of rRNA molecules and in microtubule-mediated functions (2,3). The sequence conservation suggests similar roles for the human DDX52.

The structure of DDX52 DEAD domain was solved at 2.1 Å resolution and it shows the usual DEAD domain structure with a central 8-stranded b-sheet sandwiched between 5 a-helices on each side. ADP was found in the active site together with Mg2+ ion. Intriguingly, additional nucleotide binding site was identified by pyrophosphate binding to the surface of the protein.

References

  1. Linder, P. (2006) Dead-box proteins: a family affair: active and passive players in RNP-remodeling. Nucleic Acids Res. 34:4168-80.
  2. Venema,J., Bousquet-Antonelli, C., Gelugne, J.P., Caizergues-Ferrer, M. & Tollervey, D. (1997) Rok1p is a putative RNA helicase required for rRNA processing. Mol. Cell. Biol. 17:3398-407.
  3. Rhee, J.Y., Lee, W.B. & Kim, J. (1998) Characterization and intracellular localization of the Rok1 protein involved in yeast cell division. Mol. Cells 8:68-74.