4GA0

Structure of the N-terminal domain of Nup358

4GA0 の概要

• エントリーDOI: 10.2210/pdb4ga0/pdb
• 関連するPDBエントリー: 4GA1 4GA2
• 分子名称: E3 SUMO-protein ligase RanBP2 (2 entities in total)
• 機能のキーワード: tpr motif, nuclear pore complex component nucleocytoplasmic transport, transport protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Nucleus : P49792
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 17354.88

構造登録者

Kassube, S.A.,Lin, D.H.,Stuwe, T.,Hoelz, A. (登録日: 2012-07-24, 公開日: 2012-09-26, 最終更新日: 2023-09-13)

主引用文献

Kassube, S.A.,Stuwe, T.,Lin, D.H.,Antonuk, C.D.,Napetschnig, J.,Blobel, G.,Hoelz, A.
Crystal structure of the N-terminal domain of Nup358/RanBP2.
J.Mol.Biol., 423:752-765, 2012

PubMed Abstract: Key steps in mRNA export are the nuclear assembly of messenger ribonucleoprotein particles (mRNPs), the translocation of mRNPs through the nuclear pore complex (NPC), and the mRNP remodeling events at the cytoplasmic side of the NPC. Nup358/RanBP2 is a constituent of the cytoplasmic filaments of the NPC specific to higher eukaryotes and provides a multitude of binding sites for the nucleocytoplasmic transport machinery. Here, we present the crystal structure of the Nup358 N-terminal domain (NTD) at 0.95Å resolution. The structure reveals an α-helical domain that harbors three central tetratricopeptide repeats (TPRs), flanked on each side by an additional solvating amphipathic α helix. Overall, the NTD adopts an unusual extended conformation that lacks the characteristic peptide-binding groove observed in canonical TPR domains. Strikingly, the vast majority of the NTD surface exhibits an evolutionarily conserved, positive electrostatic potential, and we demonstrate that the NTD possesses the capability to bind single-stranded RNA in solution. Together, these data suggest that the NTD contributes to mRNP remodeling events at the cytoplasmic face of the NPC.

PubMed: 22959972
DOI: 10.1016/j.jmb.2012.08.026

実験手法

X-RAY DIFFRACTION (1.15 Å)