3ewe | pdb_00003ewe

Crystal Structure of the Nup85/Seh1 Complex

spinqualitylabelsall models 3ewe, resolution 3.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 3ewe is a 4 chain structure with sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 3.5Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function SEH1_YEAST Functions as a component of the nuclear pore complex (NPC). NPC components, collectively referred to as nucleoporins (NUPs), can play the role of both NPC structural components and of docking or interaction partners for transiently associated nuclear transport factors. Involved in nuclear poly(A)+ RNA export and NPC biogenesis. It is also required for normal nuclear morphology. Component of the SEA complex which coats the vacuolar membrane and is involved in intracellular trafficking, autophagy, response to nitrogen starvation, and amino acid biogenesis. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Nuclear pore complexes (NPCs) facilitate nucleocytoplasmic transport. These massive assemblies comprise an eight-fold symmetric scaffold of architectural proteins and central-channel phenylalanine-glycine-repeat proteins forming the transport barrier. We determined the Nup85*Seh1 structure, a module in the heptameric Nup84 complex, at 3.5 A 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 identify interactions that define the organization of the Nup84 complex based on comparison with vesicle coats and confirmed the sites by mutagenesis. We propose the NPC scaffold, like vesicle coats, is composed of polygons with vertices and edges forming a membrane-proximal lattice providing docking sites for additional nucleoporins. Structural Evidence for Common Ancestry of the Nuclear Pore Complex and Vesicle Coats.,Brohawn SG, Leksa NC, Spear ED, Rajashankar KR, Schwartz TU Science. 2008 Oct 30. PMID:18974315 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Nucleoporin 3D structures

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