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5CWW

Crystal structure of the Chaetomium thermophilum heterotrimeric Nup82 NTD-Nup159 TAIL-Nup145N APD complex

Summary for 5CWW
Entry DOI10.2210/pdb5cww/pdb
Related5CWS 5CWT 5CWU 5CWV
DescriptorNucleoporin NUP145N, Nucleoporin NUP82, Nucleoporin NUP159, ... (4 entities in total)
Functional Keywordsnucleocytoplasmic transport, transport protein
Biological sourceChaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
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Total number of polymer chains3
Total formula weight85096.05
Authors
Primary citationStuwe, T.,Bley, C.J.,Thierbach, K.,Petrovic, S.,Schilbach, S.,Mayo, D.J.,Perriches, T.,Rundlet, E.J.,Jeon, Y.E.,Collins, L.N.,Huber, F.M.,Lin, D.H.,Paduch, M.,Koide, A.,Lu, V.,Fischer, J.,Hurt, E.,Koide, S.,Kossiakoff, A.A.,Hoelz, A.
Architecture of the fungal nuclear pore inner ring complex.
Science, 350:56-64, 2015
Cited by
PubMed Abstract: The nuclear pore complex (NPC) constitutes the sole gateway for bidirectional nucleocytoplasmic transport. We present the reconstitution and interdisciplinary analyses of the ~425-kilodalton inner ring complex (IRC), which forms the central transport channel and diffusion barrier of the NPC, revealing its interaction network and equimolar stoichiometry. The Nsp1•Nup49•Nup57 channel nucleoporin heterotrimer (CNT) attaches to the IRC solely through the adaptor nucleoporin Nic96. The CNT•Nic96 structure reveals that Nic96 functions as an assembly sensor that recognizes the three-dimensional architecture of the CNT, thereby mediating the incorporation of a defined CNT state into the NPC. We propose that the IRC adopts a relatively rigid scaffold that recruits the CNT to primarily form the diffusion barrier of the NPC, rather than enabling channel dilation.
PubMed: 26316600
DOI: 10.1126/science.aac9176
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.2 Å)
Structure validation

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