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TitleCryo-EM structure of the inner ring from the Xenopus laevis nuclear pore complex.
Journal, issue, pagesCell Res, Vol. 32, Issue 5, Page 451-460, Year 2022
Publish dateMar 18, 2022
AuthorsGaoxingyu Huang / Xiechao Zhan / Chao Zeng / Ke Liang / Xuechen Zhu / Yanyu Zhao / Pan Wang / Qifan Wang / Qiang Zhou / Qinghua Tao / Minhao Liu / Jianlin Lei / Chuangye Yan / Yigong Shi /
PubMed AbstractNuclear 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 ...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.
External linksCell Res / PubMed:35301439 / PubMed Central
MethodsEM (single particle)
Resolution4.2 Å
Structure data

32566

7wkk

EMDB-32566, PDB-7wkk:
Cryo-EM structure of the IR subunit from X. laevis NPC
Method: EM (single particle) / Resolution: 4.2 Å

Source
  • xenopus laevis (African clawed frog)
  • African clawed frog (African clawed frog)
KeywordsSTRUCTURAL PROTEIN / nuclear pore complex / inner ring / Nup205 / Nup93 / Nup188 / Nup155 / NDC1 / Aladin

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