3F3P

Crystal structure of the nucleoporin pair Nup85-Seh1, space group P21212

Summary for 3F3P

• Entry DOI: 10.2210/pdb3f3p/pdb
• Related: 3F3F 3F3G
• Descriptor: Nucleoporin SEH1, Nucleoporin NUP85 (2 entities in total)
• Functional Keywords: structural 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 source: Saccharomyces cerevisiae; More
• Cellular location: Nucleus, nuclear pore complex : P53011 P46673
• Total number of polymer chains: 12
• Total formula weight: 631920.35

Authors

Debler, E.W.,Hseo, H.,Ma, Y.,Blobel, G.,Hoelz, A. (deposition date: 2008-10-31, release date: 2009-04-07, Last modification date: 2024-11-13)

Primary citation

Debler, 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

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

Experimental method

X-RAY DIFFRACTION (3.2 Å)