3NV0

Crystal structure and mutational analysis of the NXF2/NXT1 heterodimeric complex from caenorhabditis elegans at 1.84 A resolution

3NV0 の概要

• エントリーDOI: 10.2210/pdb3nv0/pdb
• 分子名称: Nuclear RNA export factor 2, NTF2-related export protein, DI(HYDROXYETHYL)ETHER, ... (7 entities in total)
• 機能のキーワード: ntf2-like domain, beta sheet heterodimer interface, nucleoporin binding pocket, water mediated interface, cation-pi interactions, pi-pi interactions, nxf-loop, ntf2-plug, intramonomer buried waters, novel surface exposed pockets, mrna transport, nucleus, rna-binding, rna binding-protein transport complex, rna binding/protein transport
• 由来する生物種: Caenorhabditis elegans (nematode); 詳細
• 細胞内の位置: Nucleus: Q9XVS8; Nucleus (By similarity): Q9U757
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 41997.40

構造登録者

Kerkow, D.E.,Carmel, A.B.,Williamson, J.R. (登録日: 2010-07-07, 公開日: 2011-07-20, 最終更新日: 2024-02-21)

主引用文献

Kerkow, D.E.,Carmel, A.B.,Menichelli, E.,Ambrus, G.,Hills, R.D.,Gerace, L.,Williamson, J.R.
The structure of the NXF2/NXT1 heterodimeric complex reveals the combined specificity and versatility of the NTF2-like fold.
J.Mol.Biol., 415:649-665, 2012

PubMed Abstract: NXF1-like members of the NXF (nuclear export factor) family orchestrate bulk nuclear export of mRNA, while functionally distinct NXF variant proteins carry out separate substrate-specific and tissue-specific RNA regulation. Metazoan organisms possess at least one NXF1-like gene and one or more NXF variant genes. Heterodimerization of both proteins with the NXT (NTF2-related export) protein is central to NXF family function; however, given the multiplicity of NXF/NXT complexes, the specificity and mechanism of heterodimerization remain unclear. Here, we report the structural and functional analyses of the Caenorhabditis elegans NXF variant ceNXF2 bound to ceNXT1. Contacts crucial for NXF/NXT heterodimer stability and specificity, including a probable site for phosphoregulation, have been identified. The ceNXF2 NTF2 domain bears at least two nucleoporin (Nup) binding pockets necessary for the colocalization of ceNXF2/ceNXT1 at the nuclear envelope. Unexpectedly, one Nup binding pocket is formed at the heterodimer interface of the ceNXF2/ceNXT1 complex, demonstrating that NXT binding directly regulates NXF function.

PubMed: 22123199
DOI: 10.1016/j.jmb.2011.11.027

実験手法

X-RAY DIFFRACTION (1.84 Å)