3FMP

Crystal structure of the nucleoporin Nup214 in complex with the DEAD-box helicase Ddx19

Summary for 3FMP

• Entry DOI: 10.2210/pdb3fmp/pdb
• Related: 3FMO
• Descriptor: Nuclear pore complex protein Nup214, ATP-dependent RNA helicase DDX19B, ADENOSINE-5'-DIPHOSPHATE (3 entities in total)
• Functional Keywords: nuclear porin, nuclear pore complex, nucleocytoplasmic transport, mrna export, protein interaction, helicase, beta-propeller, dead box, glycoprotein, mrna transport, nucleus, phosphoprotein, protein transport, proto-oncogene, translocation, transport, atp-binding, hydrolase, membrane, nucleotide-binding, rna-binding, protein transport-hydrolase complex, oncoprotein-hydrolase complex, oncoprotein/hydrolase
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus, nuclear pore complex : P35658; Cytoplasm: Q9UMR2
• Total number of polymer chains: 4
• Total formula weight: 208303.90

Authors

Napetschnig, J.,Debler, E.W.,Blobel, G.,Hoelz, A. (deposition date: 2008-12-22, release date: 2009-05-19, Last modification date: 2023-09-06)

Primary citation

Napetschnig, J.,Kassube, S.A.,Debler, E.W.,Wong, R.W.,Blobel, G.,Hoelz, A.
Structural and functional analysis of the interaction between the nucleoporin Nup214 and the DEAD-box helicase Ddx19.
Proc.Natl.Acad.Sci.USA, 106:3089-3094, 2009

PubMed Abstract: Key steps in the export of mRNA from the nucleus to the cytoplasm are the transport through the nuclear pore complex (NPC) and the subsequent remodeling of messenger RNA-protein (mRNP) complexes that occurs at the cytoplasmic side of the NPC. Crucial for these events is the recruitment of the DEAD-box helicase Ddx19 to the cytoplasmic filaments of the NPC that is mediated by the nucleoporin Nup214. Here, we present the crystal structure of the Nup214 N-terminal domain in complex with Ddx19 in its ADP-bound state at 2.5 A resolution. Strikingly, the interaction surfaces are not only evolutionarily conserved but also exhibit strongly opposing surface potentials, with the helicase surface being positively and the Nup214 surface being negatively charged. We speculate that the positively charged surface of the interacting ADP-helicase binds competitively to a segment of mRNA of a linearized mRNP, passing through the NPC on its way to the cytoplasm. As a result, the ADP-helicase would dissociate from Nup214 and replace a single bound protein from the mRNA. One cycle of protein replacement would be accompanied, cooperatively, by nucleotide exchange, ATP hydrolysis, release of the ADP-helicase from mRNA and its rebinding to Nup214. Repeat of these cycles would remove proteins from a mRNP, one at a time, akin to a ratchet mechanism for mRNA export.

PubMed: 19208808
DOI: 10.1073/pnas.0813267106

Experimental method

X-RAY DIFFRACTION (3.19 Å)