3EWE

Crystal Structure of the Nup85/Seh1 Complex

Summary for 3EWE

• Entry DOI: 10.2210/pdb3ewe/pdb
• Descriptor: Nucleoporin SEH1, Nucleoporin NUP85 (2 entities in total)
• Functional Keywords: nucleoporin, nuclear pore complex, mrna transport, nucleus, protein transport, translocation, cell membrane, membrane, phosphoprotein, transport, wd repeat, membrane protein, structural protein
• Biological source: Saccharomyces cerevisiae (Baker's yeast,yeast); More
• Cellular location: Nucleus, nuclear pore complex: P53011 P46673
• Total number of polymer chains: 4
• Total formula weight: 206758.32

Authors

Brohawn, S.G.,Leksa, N.C.,Rajashankar, K.R.,Schwartz, T.U. (deposition date: 2008-10-14, release date: 2008-11-11, Last modification date: 2024-10-09)

Primary citation

Brohawn, S.G.,Leksa, N.C.,Spear, E.D.,Rajashankar, K.R.,Schwartz, T.U.
Structural evidence for common ancestry of the nuclear pore complex and vesicle coats.
Science, 322:1369-1373, 2008

PubMed Abstract: Nuclear pore complexes (NPCs) facilitate nucleocytoplasmic transport. These massive assemblies comprise an eightfold symmetric scaffold of architectural proteins and central-channel phenylalanine-glycine-repeat proteins forming the transport barrier. We determined the nucleoporin 85 (Nup85)*Seh1 structure, a module in the heptameric Nup84 complex, at 3.5 angstroms resolution. Structural, biochemical, and genetic analyses position the Nup84 complex in two peripheral NPC rings. We establish a conserved tripartite element, the ancestral coatomer element ACE1, that reoccurs in several nucleoporins and vesicle coat proteins, providing structural evidence of coevolution from a common ancestor. We identified interactions that define the organization of the Nup84 complex on the basis of comparison with vesicle coats and confirmed the sites by mutagenesis. We propose that the NPC scaffold, like vesicle coats, is composed of polygons with vertices and edges forming a membrane-proximal lattice that provides docking sites for additional nucleoporins.

PubMed: 18974315
DOI: 10.1126/science.1165886

Experimental method

X-RAY DIFFRACTION (3.5 Å)