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7WB4

Cryo-EM structure of the NR subunit from X. laevis NPC

Summary for 7WB4
Entry DOI10.2210/pdb7wb4/pdb
EMDB information32394
Descriptorouter Nup133, Nuclear pore complex protein, Nuclear pore complex protein Nup93, ... (13 entities in total)
Functional Keywordsnuclear pore complex, nuclear ring, nup205, nup93, y complex, elys, structural protein
Biological sourceXenopus laevis (African clawed frog)
More
Total number of polymer chains27
Total formula weight2926538.67
Authors
Huang, G.,Zhan, X.,Shi, Y. (deposition date: 2021-12-15, release date: 2022-03-02, Last modification date: 2024-06-26)
Primary citationHuang, G.,Zhan, X.,Zeng, C.,Zhu, X.,Liang, K.,Zhao, Y.,Wang, P.,Wang, Q.,Zhou, Q.,Tao, Q.,Liu, M.,Lei, J.,Yan, C.,Shi, Y.
Cryo-EM structure of the nuclear ring from Xenopus laevis nuclear pore complex.
Cell Res., 32:349-358, 2022
Cited by
PubMed Abstract: Nuclear pore complex (NPC) shuttles cargo across the nuclear envelope. Here we present single-particle cryo-EM structure of the nuclear ring (NR) subunit from Xenopus laevis NPC at an average resolution of 5.6 Å. The NR subunit comprises two 10-membered Y complexes, each with the nucleoporin ELYS closely associating with Nup160 and Nup37 of the long arm. Unlike the cytoplasmic ring (CR) or inner ring (IR), the NR subunit contains only one molecule each of Nup205 and Nup93. Nup205 binds both arms of the Y complexes and interacts with the stem of inner Y complex from the neighboring subunit. Nup93 connects the stems of inner and outer Y complexes within the same NR subunit, and places its N-terminal extended helix into the axial groove of Nup205 from the neighboring subunit. Together with other structural information, we have generated a composite atomic model of the central ring scaffold that includes the NR, IR, and CR. The IR is connected to the two outer rings mainly through Nup155. This model facilitates functional understanding of vertebrate NPC.
PubMed: 35177819
DOI: 10.1038/s41422-021-00610-w
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (5.6 Å)
Structure validation

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