5CWT

Crystal structure of Chaetomium thermophilum Nup57

Summary for 5CWT

• Entry DOI: 10.2210/pdb5cwt/pdb
• Related: 5CWU 5CWV 5CWW
• Descriptor: Nucleoporin NUP57 (2 entities in total)
• Functional Keywords: nucleocytoplasmic transport, transport protein
• Biological source: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)
• Total number of polymer chains: 4
• Total formula weight: 25199.63

Authors

Bley, C.J.,Hoelz, A. (deposition date: 2015-07-28, release date: 2015-09-16, Last modification date: 2024-03-06)

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

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

Experimental method

X-RAY DIFFRACTION (2.5 Å)