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7WOO

Cryo-EM structure of the inner ring protomer of the Saccharomyces cerevisiae nuclear pore complex

Summary for 7WOO
Entry DOI10.2210/pdb7woo/pdb
EMDB information32653
DescriptorNucleoporin NIC96, Nucleoporin NUP157, Nucleoporin NUP170, ... (8 entities in total)
Functional Keywordsnuclear pore complex, inner ring, protomer, saccharomyces cerevisiae, transport protein
Biological sourceSaccharomyces cerevisiae (baker's yeast)
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Total number of polymer chains12
Total formula weight1286201.19
Authors
Li, Z.Q.,Chen, S.J.B.,Zhao, L.,Sui, S.F. (deposition date: 2022-01-22, release date: 2022-04-13, Last modification date: 2024-06-26)
Primary citationLi, 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
Cited by
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
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.71 Å)
Structure validation

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