2RFO

Crystral Structure of the nucleoporin Nic96

Summary for 2RFO

• Entry DOI: 10.2210/pdb2rfo/pdb
• Descriptor: Nucleoporin NIC96 (2 entities in total)
• Functional Keywords: alpha-alpha-superhelix, mrna transport, nuclear pore complex, nucleus, protein transport, translocation, transport, structural protein
• Biological source: Saccharomyces cerevisiae (baker's yeast)
• Cellular location: Nucleus, nuclear pore complex: P34077
• Total number of polymer chains: 2
• Total formula weight: 149638.50

Authors

Schrader, N.,Stelter, P.,Flemming, D.,Kunze, K.,Hurt, E.,Vetter, I.R. (deposition date: 2007-10-01, release date: 2008-01-29, Last modification date: 2024-03-13)

Primary citation

Schrader, N.,Stelter, P.,Flemming, D.,Kunze, R.,Hurt, E.,Vetter, I.R.
Structural basis of the nic96 subcomplex organization in the nuclear pore channel.
Mol.Cell, 29:46-55, 2008

PubMed Abstract: Nic96 is a conserved nucleoporin that recruits the Nsp1-Nup49-Nup57 complex, a module with Phe-Gly (FG) repeats, to the central transport channel of the nuclear pore complex (NPC). Nic96 binds the Nsp1 complex via its N domain and assembles into the NPC framework via its central and C domain. Here, we report the crystal structure of a large structural nucleoporin, Nic96 without its N domain (Nic96DeltaN). Nic96DeltaN is composed of three domains and is a straight molecule that--although almost entirely helical--exhibits strong deviations from the predicted alpha-solenoid fold. The missing N domain projects midway from the Nic96 molecule, indicating how the Nsp1 complex might be located with respect to the rod-like Nic96. Notably, Nic96DeltaN binds in vitro to FG repeats of the Nsp1 complex. These data suggest a model of how Nic96 could organize a transport module with coiled-coil domains and FG repeats in the central pore channel.

PubMed: 18206968
DOI: 10.1016/j.molcel.2007.10.022

Experimental method

X-RAY DIFFRACTION (2.6 Å)