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5HB4

Crystal structure of Chaetomium thermophilum Nup192

Summary for 5HB4
Entry DOI10.2210/pdb5hb4/pdb
Related5HAX 5HAY 5HAZ 5HB0 5HB1 5HB2 5HB3 5HB5 5HB6 5HB7 5HB8
DescriptorNup192,Nucleoporin NUP192, OSMIUM ION (2 entities in total)
Functional Keywordsnucleocytoplasmic transport, protein transport, transport protein
Biological sourceChaetomium thermophilum
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Total number of polymer chains1
Total formula weight179380.42
Authors
Stuwe, T.,Lin, D.H.,Hoelz, A. (deposition date: 2015-12-31, release date: 2016-04-20, Last modification date: 2024-03-06)
Primary citationLin, D.H.,Stuwe, T.,Schilbach, S.,Rundlet, E.J.,Perriches, T.,Mobbs, G.,Fan, Y.,Thierbach, K.,Huber, F.M.,Collins, L.N.,Davenport, A.M.,Jeon, Y.E.,Hoelz, A.
Architecture of the symmetric core of the nuclear pore.
Science, 352:aaf1015-aaf1015, 2016
Cited by
PubMed Abstract: The nuclear pore complex (NPC) controls the transport of macromolecules between the nucleus and cytoplasm, but its molecular architecture has thus far remained poorly defined. We biochemically reconstituted NPC core protomers and elucidated the underlying protein-protein interaction network. Flexible linker sequences, rather than interactions between the structured core scaffold nucleoporins, mediate the assembly of the inner ring complex and its attachment to the NPC coat. X-ray crystallographic analysis of these scaffold nucleoporins revealed the molecular details of their interactions with the flexible linker sequences and enabled construction of full-length atomic structures. By docking these structures into the cryoelectron tomographic reconstruction of the intact human NPC and validating their placement with our nucleoporin interactome, we built a composite structure of the NPC symmetric core that contains ~320,000 residues and accounts for ~56 megadaltons of the NPC's structured mass. Our approach provides a paradigm for the structure determination of similarly complex macromolecular assemblies.
PubMed: 27081075
DOI: 10.1126/science.aaf1015
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3.2 Å)
Structure validation

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