| Title | 8 angstrom structure of the outer rings of the Xenopus laevis nuclear pore complex obtained by cryo-EM and AI |
| Authors | Tai, Linhua Zhu, Yun Ren, He Huang, Xiaojun Zhang, Chuanmao Sun, Fei |
| Affiliation | Chinese Acad Sci, CAS Ctr Excellence Biomacromol, Inst Biophys, Natl Key Lab Biomacromol, Beijing 100101, Peoples R China Peking Univ, Coll Life Sci, Minist Educ, Key Lab Cell Proliferat & Differentiat, Beijing 100871, Peoples R China Peking Univ, Coll Life Sci, State Key Lab Membrane Biol, Beijing 100871, Peoples R China Chinese Acad Sci, Ctr Biol Imaging, Inst Biophys, Beijing 100101, Peoples R China Univ Chinese Acad Sci, Beijing 100049, Peoples R China Guangzhou Regenerat Med & Hlth Guangdong Lab, Bioland Lab, Guangzhou 510005, Peoples R China |
| Keywords | N-TERMINAL DOMAIN FUNCTIONAL-ANALYSIS NUCLEOPORIN NUP214 CRYSTAL-STRUCTURE BINDING-SITES ARCHITECTURE DYNAMICS VISUALIZATION SCAFFOLD COAT |
| Issue Date | Jan-2022 |
| Publisher | PROTEIN & CELL |
| 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 angstrom 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 angstrom. 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. |
| URI | http://hdl.handle.net/20.500.11897/634764 |
| ISSN | 1674-800X |
| DOI | 10.1007/s13238-021-00895-y |
| Indexed | SCI(E) |
| Appears in Collections: | 生命科学学院 细胞增殖分化调控机理研究教育部重点实验室 膜生物学国家重点实验室 |
