6LK8

Structure of Xenopus laevis Cytoplasmic Ring subunit.

Summary for 6LK8

• Entry DOI: 10.2210/pdb6lk8/pdb
• Related: 5HB4
• EMDB information: 0909
• Descriptor: MGC83295 protein, outer Nup133, Nup358 complex, clamps, ... (18 entities in total)
• Functional Keywords: building block of vertebrate npc., structural protein
• Biological source: Xenopus laevis (African clawed frog); More
• Total number of polymer chains: 32
• Total formula weight: 3291331.20

Authors

Shi, Y.,Huang, G.,Yan, C.,Zhang, Y. (deposition date: 2019-12-18, release date: 2021-07-21, Last modification date: 2024-05-29)

Primary citation

Huang, G.,Zhang, Y.,Zhu, X.,Zeng, C.,Wang, Q.,Zhou, Q.,Tao, Q.,Liu, M.,Lei, J.,Yan, C.,Shi, Y.
Structure of the cytoplasmic ring of the Xenopus laevis nuclear pore complex by cryo-electron microscopy single particle analysis.
Cell Res., 30:520-531, 2020

PubMed 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.

PubMed: 32376910
DOI: 10.1038/s41422-020-0319-4

Experimental method

ELECTRON MICROSCOPY (5.5 Å)