3FHC

Crystal structure of human Dbp5 in complex with Nup214

3FHC の概要

• エントリーDOI: 10.2210/pdb3fhc/pdb
• 関連するPDBエントリー: 2OIT 3FHT
• 分子名称: Nuclear pore complex protein Nup214, ATP-dependent RNA helicase DDX19B (3 entities in total)
• 機能のキーワード: 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
• 由来する生物種: Homo sapiens (human); 詳細
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 71522.53

構造登録者

von Moeller, H.,Conti, E. (登録日: 2008-12-09, 公開日: 2009-02-17, 最終更新日: 2023-11-01)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.8 Å)