Journal
CELL RESEARCH
Volume 30, Issue 6, Pages 520-531Publisher
SPRINGERNATURE
DOI: 10.1038/s41422-020-0319-4
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Funding
- Westlake University
- National Natural Science Foundation of China [31930059, 81920108015, 31621092, 31430020]
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The nuclear pore complex (NPC) exhibits structural plasticity and has only been characterized at local resolutions of up to 15 angstrom for the cytoplasmic ring (CR). Here we present a single-particle cryo-electron microscopy (cryo-EM) structure of the CR from Xenopus laevis NPC at average resolutions of 5.5-7.9 angstrom, with local resolutions reaching 4.5 angstrom. Improved resolutions allow identification and placement of secondary structural elements in the majority of the CR components. The two Y complexes in each CR subunit interact with each other and associate with those from flanking subunits, forming a circular scaffold. Within each CR subunit, the Nup358-containing region wraps around the stems of both Y complexes, likely stabilizing the scaffold. Nup205 connects the short arms of the two Y complexes and associates with the stem of a neighboring Y complex. The Nup214-containing region uses an extended coiled-coil to link Nup85 of the two Y complexes and protrudes into the axial pore of the NPC. These previously uncharacterized structural features reveal insights into NPC assembly.
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