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TitleNear-atomic structure of the inner ring of the Saccharomyces cerevisiae nuclear pore complex.
Journal, issue, pagesCell Res, Vol. 32, Issue 5, Page 437-450, Year 2022
Publish dateMar 18, 2022
AuthorsZongqiang Li / Shuaijiabin Chen / Liang Zhao / Guoqiang Huang / Xiong Pi / Shan Sun / Peiyi Wang / Sen-Fang Sui /
PubMed AbstractNuclear pore complexes (NPCs) mediate bidirectional nucleocytoplasmic transport of substances in eukaryotic cells. However, the accurate molecular arrangement of NPCs remains enigmatic owing to their ...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.
External linksCell Res / PubMed:35301440 / PubMed Central
MethodsEM (single particle)
Resolution2.81 - 12.03 Å
Structure data

32643

7wo9

EMDB-32643, PDB-7wo9:
Cryo-EM structure of full-length Nup188
Method: EM (single particle) / Resolution: 2.81 Å

EMDB-32644: Cryo-EM structure of full-length Nup188 (multiBody refined N-terminal region)
Method: EM (single particle) / Resolution: 3.02 Å

EMDB-32645: Cryo-EM structure of full-length Nup188 (multibody refined C-terminal region)
Method: EM (single particle) / Resolution: 3.41 Å

32653

7woo

EMDB-32653, PDB-7woo:
Cryo-EM structure of the inner ring protomer of the Saccharomyces cerevisiae nuclear pore complex
Method: EM (single particle) / Resolution: 3.71 Å

32658

7wot

EMDB-32658, PDB-7wot:
Cryo-EM structure of the inner ring monomer of the Saccharomyces cerevisiae nuclear pore complex
Method: EM (single particle) / Resolution: 3.73 Å

EMDB-32662: Cryo-EM map of the inner ring dimer of the Saccharomyces cerevisiae nuclear pore complex
Method: EM (single particle) / Resolution: 7.69 Å

EMDB-32663: Cryo-EM map of the intact inner ring of the Saccharomyces cerevisiae nuclear pore complex
Method: EM (single particle) / Resolution: 9.1 Å

EMDB-32664: Cryo-EM map of the whole Saccharomyces cerevisiae nuclear pore complex
Method: EM (single particle) / Resolution: 12.03 Å

Source
  • saccharomyces cerevisiae s288c (yeast)
  • saccharomyces cerevisiae (brewer's yeast)
KeywordsTRANSPORT PROTEIN / Nup188 / cryo-EM / Saccharomyces cerevisiae / nuclear pore complex / inner ring / protomer / monomer

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