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 DOI | 10.2210/pdb7vop/pdb |
EMDB information | 32056 |
Descriptor | Nuclear pore complex protein Nup85, MGC83295 protein, Nuclear pore complex protein Nup93, ... (15 entities in total) |
Functional Keywords | cytoplasmic ring, cryo-em, nuclear pore complex, xenopus laevis, nuclear protein |
Biological source | Xenopus laevis (African clawed frog) More |
Total number of polymer chains | 32 |
Total formula weight | 4326615.04 |
Authors | |
Primary citation | Tai, 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: 35015240DOI: 10.1007/s13238-021-00895-y PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.7 Å) |
Structure validation
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