EMD-31891

Single-particle
8.1 Å
EMD-31891 Deposition: 03/09/2021
Map released: 02/02/2022
Last modified: 19/06/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links

EMD-31891

Structure of Xenopus laevis NPC nuclear ring asymmetric unit

EMD-31891

Single-particle
8.1 Å
EMD-31891 Deposition: 03/09/2021
Map released: 02/02/2022
Last modified: 19/06/2024
Overview 3D View Sample Experiment Validation Volume Browser Additional data Links
Sample Organism: Xenopus laevis
Sample: nuclear pore complex
Fitted models: 7vci (Avg. Q-score: 0.13)

Deposition Authors: Tai L , Zhu Y
8 angstrom structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI.
Tai L , Zhu Y , Ren H , Huang X , Zhang C , Sun F
(2022) Protein Cell , 13 , 760 - 777
PUBMED: 35015240
DOI: doi:10.1007/s13238-021-00895-y
ISSN: 1674-8018
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.