3FHC

Crystal structure of human Dbp5 in complex with Nup214

Summary for 3FHC

• Entry DOI: 10.2210/pdb3fhc/pdb
• Related: 2OIT 3FHT
• Descriptor: Nuclear pore complex protein Nup214, ATP-dependent RNA helicase DDX19B (3 entities in total)
• Functional Keywords: dead-box helicase, mrna export, nucleoporin, beta propeller, reca-like, rna dependent atpase, can, ddx19, dead-box protein 19b, nuclear pore complex, glycoprotein, mrna transport, nucleus, phosphoprotein, protein transport, proto-oncogene, translocation, transport, atp-binding, helicase, hydrolase, membrane, nucleotide-binding, rna-binding, transport protein-hydrolase complex, transport protein/hydrolase
• Biological source: Homo sapiens (human); More
• Total number of polymer chains: 2
• Total formula weight: 71522.53

Authors

von Moeller, H.,Conti, E. (deposition date: 2008-12-09, release date: 2009-02-17, Last modification date: 2023-11-01)

Primary citation

von Moeller, H.,Basquin, C.,Conti, E.
The mRNA export protein DBP5 binds RNA and the cytoplasmic nucleoporin NUP214 in a mutually exclusive manner
Nat.Struct.Mol.Biol., 16:247-254, 2009

PubMed Abstract: The DEAD-box protein DBP5 is essential for mRNA export in both yeast and humans. It binds RNA and is concentrated and locally activated at the cytoplasmic side of the nuclear pore complex. We have determined the crystal structures of human DBP5 bound to RNA and AMPPNP, and bound to the cytoplasmic nucleoporin NUP214. The structures reveal that binding of DBP5 to nucleic acid and to NUP214 is mutually exclusive. Using in vitro assays, we demonstrate that NUP214 decreases both the RNA binding and ATPase activities of DBP5. The interactions are mediated by conserved residues, implying a conserved recognition mechanism. These results suggest a framework for the consecutive steps leading to the release of mRNA at the final stages of nuclear export. More generally, they provide a paradigm for how binding of regulators can specifically inhibit DEAD-box proteins.

PubMed: 19219046
DOI: 10.1038/nsmb.1561

Experimental method

X-RAY DIFFRACTION (2.8 Å)