4I9Y

Structure of the C-terminal domain of Nup358

Summary for 4I9Y

• Entry DOI: 10.2210/pdb4i9y/pdb
• Related: 4IF5 4IF6 4IG9
• Descriptor: E3 SUMO-protein ligase RanBP2, GLYCEROL, CHLORIDE ION, ... (5 entities in total)
• Functional Keywords: nuclear pore complex, transport protein
• Biological source: Homo sapiens (human)
• Cellular location: Nucleus : P49792
• Total number of polymer chains: 6
• Total formula weight: 112917.94

Authors

Lin, D.H.,Zimmermann, S.,Stuwe, T.,Stuwe, E.,Hoelz, A. (deposition date: 2012-12-05, release date: 2013-01-30, Last modification date: 2024-10-16)

Primary citation

Lin, D.H.,Zimmermann, S.,Stuwe, T.,Stuwe, E.,Hoelz, A.
Structural and Functional Analysis of the C-Terminal Domain of Nup358/RanBP2.
J.Mol.Biol., 425:1318-1329, 2013

PubMed Abstract: The nuclear pore complex is the sole mediator of bidirectional transport between the nucleus and cytoplasm. Nup358 is a metazoan-specific nucleoporin that localizes to the cytoplasmic filaments and provides several binding sites for the mobile nucleocytoplasmic transport machinery. Here we present the crystal structure of the C-terminal domain (CTD) of Nup358 at 1.75Å resolution. The structure reveals that the CTD adopts a cyclophilin-like fold with a non-canonical active-site configuration. We determined biochemically that the CTD possesses weak peptidyl-prolyl isomerase activity and show that the active-site cavity mediates a weak association with the human immunodeficiency virus-1 capsid protein, supporting its role in viral infection. Overall, the surface is evolutionarily conserved, suggesting that the CTD serves as a protein-protein interaction platform. However, we demonstrate that the CTD is dispensable for nuclear envelope localization of Nup358, suggesting that the CTD does not interact with other nucleoporins.

PubMed: 23353830
DOI: 10.1016/j.jmb.2013.01.021

Experimental method

X-RAY DIFFRACTION (1.75 Å)