Volume 32, No 5, May 2022

ISSN: 1001-0602 
EISSN: 1748-7838 2018 
impact factor 17.848* 
(Clarivate Analytics, 2019)

Volume 32 Issue 5, May 2022: 448-460   |  Open Access

ORIGINAL ARTICLES

Cryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex

Gaoxingyu Huang^1,2,3,†,* , Xiechao Zhan^1,2,3,† , Chao Zeng^1,2,3,† , Ke Liang^1,2,3,† , Xuechen Zhu^1,2,3,† , Yanyu Zhao^1,2,3 , Pan Wang^4,5 , Qifan Wang^1,2,3 , Qiang Zhou^1,2,3 , Qinghua Tao⁴ , Minhao Liu⁴ , Jianlin Lei⁴ , Chuangye Yan^4,5 , Yigong Shi^1,2,3,4,5,*

¹Westlake Laboratory of Life Sciences and Biomedicine, Hangzhou, Zhejiang, China
²Key Laboratory of Structural Biology of Zhejiang Province, School of Life Sciences, Westlake University, Hangzhou, Zhejiang, China
³Institute of Biology, Westlake Institute for Advanced Study, 18 Shilongshan Road, Hangzhou, Zhejiang, China
⁴Beijing Advanced Innovation Center for Structural Biology & Frontier Research Center for Biological Structure, Beijing, China
⁵Tsinghua University-Peking University Joint Center for Life Sciences; School of Life Sciences, Tsinghua University, Beijing, China
^†These authors contributed equally: Gaoxingyu Huang, Xiechao Zhan, Chao Zeng, Ke Liang, Xuechen Zhu
Correspondence: Gaoxingyu Huang(huanggaoxingyu@westlake.edu.cn)Yigong Shi(syg@westlake.edu.cn)

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.

https://doi.org/10.1038/s41422-022-00633-x

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