7WO9

Cryo-EM structure of full-length Nup188

Summary for 7WO9

• Entry DOI: 10.2210/pdb7wo9/pdb
• EMDB information: 32643
• Descriptor: Nucleoporin NUP188 (1 entity in total)
• Functional Keywords: nup188, cryo-em, saccharomyces cerevisiae, transport protein
• Biological source: Saccharomyces cerevisiae S288C
• Total number of polymer chains: 1
• Total formula weight: 188753.28

Authors

Zhao, L.,Li, Z.Q.,Sui, S.F. (deposition date: 2022-01-20, release date: 2022-03-30, Last modification date: 2024-06-26)

Primary citation

Li, Z.,Chen, S.,Zhao, L.,Huang, G.,Pi, X.,Sun, S.,Wang, P.,Sui, S.F.
Near-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex.
Cell Res., 32:437-450, 2022

PubMed Abstract: Nuclear pore complexes (NPCs) mediate bidirectional nucleocytoplasmic transport of substances in eukaryotic cells. However, the accurate molecular arrangement of NPCs remains enigmatic owing to their huge size and highly dynamic nature. Here we determined the structure of the asymmetric unit of the inner ring (IR monomer) at 3.73 Å resolution by single-particle cryo-electron microscopy, and created an atomic model of the intact IR consisting of 192 molecules of 8 nucleoporins. In each IR monomer, the Z-shaped Nup188-Nup192 complex in the middle layer is sandwiched by two approximately parallel rhomboidal structures in the inner and outer layers, while Nup188, Nup192 and Nic96 link all subunits to constitute a relatively stable IR monomer. In contrast, the intact IR is assembled by loose and instable interactions between IR monomers. These structures, together with previously reported structural information of IR, reveal two distinct interaction modes between IR monomers and extensive flexible connections in IR assembly, providing a structural basis for the stability and malleability of IR.

PubMed: 35301440
DOI: 10.1038/s41422-022-00632-y

Experimental method

ELECTRON MICROSCOPY (2.81 Å)