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7VOP

Cryo-EM structure of Xenopus laevis nuclear pore complex cytoplasmic ring subunit

This is a non-PDB format compatible entry.
Summary for 7VOP
Entry DOI10.2210/pdb7vop/pdb
EMDB information32056
DescriptorNuclear pore complex protein Nup85, MGC83295 protein, Nuclear pore complex protein Nup93, ... (15 entities in total)
Functional Keywordscytoplasmic ring, cryo-em, nuclear pore complex, xenopus laevis, nuclear protein
Biological sourceXenopus laevis (African clawed frog)
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Total number of polymer chains32
Total formula weight4326615.04
Authors
Tai, L.,Zhu, Y.,Sun, F. (deposition date: 2021-10-14, release date: 2022-02-02, Last modification date: 2024-06-19)
Primary citationTai, L.,Zhu, Y.,Ren, H.,Huang, X.,Zhang, C.,Sun, F.
8 angstrom structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.
Protein Cell, 13:760-777, 2022
Cited by
PubMed Abstract: The nuclear pore complex (NPC), one of the largest protein complexes in eukaryotes, serves as a physical gate to regulate nucleocytoplasmic transport. Here, we determined the 8 Å resolution cryo-electron microscopic (cryo-EM) structure of the outer rings containing nuclear ring (NR) and cytoplasmic ring (CR) from the Xenopus laevis NPC, with local resolutions reaching 4.9 Å. With the aid of AlphaFold2, we managed to build a pseudoatomic model of the outer rings, including the Y complexes and flanking components. In this most comprehensive and accurate model of outer rings to date, the almost complete Y complex structure exhibits much tighter interaction in the hub region. In addition to two copies of Y complexes, each asymmetric subunit in CR contains five copies of Nup358, two copies of the Nup214 complex, two copies of Nup205 and one copy of newly identified Nup93, while that in NR contains one copy of Nup205, one copy of ELYS and one copy of Nup93. These in-depth structural features represent a great advance in understanding the assembly of NPCs.
PubMed: 35015240
DOI: 10.1007/s13238-021-00895-y
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (8.7 Å)
Structure validation

236371

数据于2025-05-21公开中

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