Article
Structure of the C-terminus of the mRNA export factor Dbp5 reveals the interaction surface for the ATPase activator Gle1.
Proceedings of the National Academy of Sciences of the United States of America - 22 Sept 2009
Dossani Zain Y, Weirich Christine S, Erzberger Jan P, Berger James M, Weis Karsten
Abstract excerpt
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...
Topics
- Adenosine Triphosphatases
- Amino Acid Sequence
- Binding Sites
- Catalysis
- Crystallization
- Crystallography, X-Ray
- DEAD-box RNA Helicases
- In Situ Hybridization
- Models, Molecular
- Molecular Sequence Data
- Mutation
- Nuclear Pore
- Nuclear Pore Complex Proteins