Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.

Abstract:

:The nuclear pore complex (NPC) exhibits structural plasticity and has only been characterized at local resolutions of up to 15 Å 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 Å, with local resolutions reaching 4.5 Å. 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.

journal_name

Cell Res

journal_title

Cell research

authors

Huang G,Zhang Y,Zhu X,Zeng C,Wang Q,Zhou Q,Tao Q,Liu M,Lei J,Yan C,Shi Y

doi

10.1038/s41422-020-0319-4

subject

Has Abstract

pub_date

2020-06-01 00:00:00

pages

520-531

issue

6

eissn

1001-0602

issn

1748-7838

pii

10.1038/s41422-020-0319-4

journal_volume

30

pub_type

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