Near-atomic Structure of the Cytoplasmic Ring of the Xenopus laevis Nuclear Pore Complex
0301 basic medicine
03 medical and health sciences
DOI:
10.1101/2022.02.14.480321
Publication Date:
2022-02-14T19:45:26Z
AUTHORS (14)
ABSTRACT
AbstractThe nuclear pore complex (NPC) mediates nucleocytoplasmic shuttling. Here we present single-particle cryo-EM structure of the cytoplasmic ring (CR) from the Xenopus laevis NPC at 4.1-4.7 Å resolutions. The structure of an N-terminal domain of Nup358 was resolved at 3.0 Å, facilitating identification of five Nup358 molecules in each CR subunit. Aside from unveiling the assembly details of the two Y-shaped multicomponent complexes (Y complexes) in each CR subunit, the improved resolutions reveal the C-terminal fragment of Nup160 to be an organizing center at the vertex of each Y complex. Our structures show that the scaffold of a CR subunit comprises five Nup358, two Nup205 and two Nup93 molecules in addition to the previously characterized Y complexes.One-Sentence SummaryImproved resolutions of the cytoplasmic ring (CR) of the Xenopus laevis nuclear pore complex reveal that five Nup358 molecules, together with two copies of interweaved Nup205, Nup93 and Y complexes, constitute the scaffold of each CR subunit.
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