4GA2

Structure of the N-terminal domain of Nup358

Summary for 4GA2

• Entry DOI: 10.2210/pdb4ga2/pdb
• Related: 4GA0 4GA1
• Descriptor: E3 SUMO-PROTEIN LIGASE RANBP2 (2 entities in total)
• Functional Keywords: tpr motif, nuclear pore complex component nucleocytoplasmic transport, transport protein
• Biological source: Pan troglodytes (Chimpanzee)
• Total number of polymer chains: 1
• Total formula weight: 17308.79

Authors

Kassube, S.A.,Lin, D.H.,Stuwe, T.,Hoelz, A. (deposition date: 2012-07-24, release date: 2012-09-26, Last modification date: 2024-02-28)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (0.95 Å)