Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.

@article{Dossani2009StructureOT,
  title={Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.},
  author={Zain Y Dossani and Christine S. Weirich and Jan Peter Erzberger and James M Berger and Karsten Weis},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2009},
  volume={106 38},
  pages={16251-6}
}
The DExD/H-box RNA-dependent ATPase Dbp5 plays an essential role in the nuclear export of mRNA. Dbp5 localizes to the nuclear pore complex, where its ATPase activity is stimulated by Gle1 and its coactivator inositol hexakisphosphate. Here, we present the crystal structure of the C-terminal domain of Dbp5, refined to 1.8 A. The structure reveals a RecA-like fold that contains two defining characteristics not present in other structurally characterized DExD/H-box proteins: a C-terminal alpha… CONTINUE READING

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