5CWS
Crystal structure of the intact Chaetomium thermophilum Nsp1-Nup49-Nup57 channel nucleoporin heterotrimer bound to its Nic96 nuclear pore complex attachment site
Summary for 5CWS
| Entry DOI | 10.2210/pdb5cws/pdb |
| Related | 4JNU 4JNV 4JO7 4JO9 4JQ5 5CWT 5CWU 5CWV 5CWW |
| Descriptor | sAB-158 Fab Light Chain, sAB-158 Fab Heavy Chain, Nucleoporin NSP1, ... (7 entities in total) |
| Functional Keywords | nucleocytoplasmic transport, protein transport |
| Biological source | Homo sapiens More |
| Total number of polymer chains | 12 |
| Total formula weight | 277743.99 |
| Authors | Bley, C.J.,Petrovic, S.,Paduch, M.,Lu, V.,Kossiakoff, A.A.,Hoelz, A. (deposition date: 2015-07-28, release date: 2015-10-14, Last modification date: 2024-10-30) |
| Primary citation | Stuwe, 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: 26316600DOI: 10.1126/science.aac9176 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.77 Å) |
Structure validation
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