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3F3F

Crystal structure of the nucleoporin pair Nup85-Seh1, space group P21

Summary for 3F3F
Entry DOI10.2210/pdb3f3f/pdb
Related3F3G 3F3P
DescriptorNucleoporin SEH1, Nucleoporin NUP85 (2 entities in total)
Functional Keywordsstructural protein, protein complex, nucleoporin, nucleoporin complex, nuclear pore complex, macromolecular assembly, membrane coat, nucleocytoplasmic transport, beta-propeller, solenoid domain, mrna transport, nucleus, protein transport, translocation, wd repeat
Biological sourceSaccharomyces cerevisiae
More
Cellular locationNucleus, nuclear pore complex: P53011 P46673
Total number of polymer chains8
Total formula weight417341.03
Authors
Debler, E.W.,Hseo, H.,Ma, Y.,Blobel, G.,Hoelz, A. (deposition date: 2008-10-30, release date: 2009-04-07, Last modification date: 2023-12-27)
Primary citationDebler, E.W.,Ma, Y.,Seo, H.S.,Hsia, K.C.,Noriega, T.R.,Blobel, G.,Hoelz, A.
A fence-like coat for the nuclear pore membrane.
Mol.Cell, 32:815-826, 2008
Cited by
PubMed Abstract: We recently proposed a cylindrical coat for the nuclear pore membrane in the nuclear pore complex (NPC). This scaffold is generated by multiple copies of seven nucleoporins. Here, we report three crystal structures of the nucleoporin pair Seh1*Nup85, which is part of the coat cylinder. The Seh1*Nup85 assembly bears resemblance in its shape and dimensions to that of another nucleoporin pair, Sec13*Nup145C. Furthermore, the Seh1*Nup85 structures reveal a hinge motion that may facilitate conformational changes in the NPC during import of integral membrane proteins and/or during nucleocytoplasmic transport. We propose that Seh1*Nup85 and Sec13*Nup145C form 16 alternating, vertical rods that are horizontally linked by the three remaining nucleoporins of the coat cylinder. Shared architectural and mechanistic principles with the COPII coat indicate a common evolutionary origin and support the notion that the NPC coat represents another class of membrane coats.
PubMed: 19111661
DOI: 10.1016/j.molcel.2008.12.001
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (2.9 Å)
Structure validation

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