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-Structure paper
タイトル | 8 Å structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI. |
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ジャーナル・号・ページ | Protein Cell, Vol. 13, Issue 10, Page 760-777, Year 2022 |
掲載日 | 2022年1月11日 |
著者 | Linhua Tai / Yun Zhu / He Ren / Xiaojun Huang / Chuanmao Zhang / Fei Sun / |
PubMed 要旨 | 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- ...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. |
リンク | Protein Cell / PubMed:35015240 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 7.8 - 8.9 Å |
構造データ | EMDB-31891, PDB-7vci: EMDB-31892: EMDB-31893: EMDB-32056, PDB-7vop: EMDB-32060: EMDB-32061: |
由来 |
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キーワード | NUCLEAR PROTEIN / nuclear pore complex / nuclear ring / asymmetric unit / cytoplasmic ring / cryo-EM / Xenopus laevis |