Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex
Open accessPublished version of a preprint
Abstract
Nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-electron microscopy structure of the inner ring (IR) subunit from the Xenopus laevis NPC at an average resolution of 4.2 Å. A homo-dimer of Nup205 resides at the center of the IR subunit, flanked by two molecules of Nup188. Four molecules of Nup93 each places an extended helix into the axial groove of Nup205 or Nup188, together constituting the central scaffold. The channel nucleoporin hetero-trimer of Nup62/58/54 is anchored on the central scaffold. Six Nup155 molecules interact with the central scaffold and together with the NDC1–ALADIN hetero-dimers anchor the IR subunit to the nuclear envelope and to outer rings. The scarce inter-subunit contacts may allow sufficient latitude in conformation and diameter of the IR. Our structure reveals the molecular basis for the IR subunit assembly of a vertebrate NPC.
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Highly accurate protein structure prediction with AlphaFold
Jumper, J., Evans, R., Pritzel, A., Green, T., Figurnov, M., Ronneberger, O., Tunyasuvunakool, K., Bates, R., Žídek, A., Potapenko, A., et al. (2021) · Nature · doi:10.1038/s41586-021-03819-2 · Cited by 43,764 · see citing works
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- Authors
- Huang, G., Zhan, X., Zeng, C., Liang, K., Zhu, X., Zhao, Y., Wang, P., Wang, Q., Zhou, Q., Tao, Q., Liu, M., Lei, J., Yan, C., & Shi, Y.
- Affiliations
- Westlake University (CN)
- Peking University (CN)
- Corresponding author
- Huang, Gaoxingyu
- Shi, Yigong
- ORCID
- Venue
- Cell Research
- Published
- 2022-03-18
- Volume
- 32
- Issue
- 5
- Pages
- 451-460
- ISSN
- 1001-0602 (ISSN-L)
- 1748-7838
- PMC
- PMC9061766
- OpenAlex
- W4221077980
- Cited by
- 33
- References
- 1
- Citations by year
- 2026: 3 · 2025: 7 · 2024: 4 · 2023: 10 · 2022: 9
- FWCI
- 2.45
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Locations
- Cell Research (publishedVersion, cc-by)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by)
- PubMed (publishedVersion)
- Funders
- Westlake University
- National Natural Science Foundation of China (31930059)
- China Postdoctoral Science Foundation (2021M692888)
- National Postdoctoral Program for Innovative Talents
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Nuclear Structure and Function
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Structural Biology › Advanced Electron Microscopy Techniques and Applications
- Keywords
- nuclear pore complex, Xenopus laevis, NUP205, Nup188, Nup93, NUP155, nucleoporins, nuclear transport, nuclear envelope, protein complex structure
- MeSH terms
- Animals, Nuclear Envelope, Xenopus laevis, Cryoelectron Microscopy, Active Transport, Cell Nucleus, Nuclear Pore, Nuclear Pore Complex Proteins, Xenopus Proteins
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