3I5P
Nup170(aa979-1502), S.cerevisiae
Summary for 3I5P
| Entry DOI | 10.2210/pdb3i5p/pdb |
| Related | 3I4R 3I5Q |
| Descriptor | Nucleoporin NUP170 (1 entity in total) |
| Functional Keywords | helical stack, membrane, mrna transport, nuclear pore complex, nucleus, phosphoprotein, protein transport, translocation, transmembrane, transport |
| Biological source | Saccharomyces cerevisiae (brewer's yeast,lager beer yeast,yeast) |
| Cellular location | Nucleus, nuclear pore complex: P38181 |
| Total number of polymer chains | 1 |
| Total formula weight | 61120.60 |
| Authors | Whittle, J.R.R.,Schwartz, T.U. (deposition date: 2009-07-06, release date: 2009-08-11, Last modification date: 2024-02-21) |
| Primary citation | Whittle, J.R.,Schwartz, T.U. Architectural nucleoporins Nup157/170 and Nup133 are structurally related and descend from a second ancestral element. J.Biol.Chem., 284:28442-28452, 2009 Cited by PubMed Abstract: The nuclear pore complex (NPC) constitutes one of the largest protein assemblies in the eukaryotic cell and forms the exclusive gateway to the nucleus. The stable, approximately 15-20-MDa scaffold ring of the NPC is built from two multiprotein complexes arranged around a central 8-fold axis. Here we present crystal structures of two large architectural units, yNup170(979-1502) and hNup107(658-925) x hNup133(517-1156), each a constituent of one of the two multiprotein complexes. Conservation of domain arrangement and of tertiary structure suggests that Nup157/170 and Nup133 derived from a common ancestor. Together with the previously established ancestral coatomer element (ACE1), these two elements constitute the major alpha-helical building blocks of the NPC scaffold and define its branched, lattice-like architecture, similar to vesicle coats like COPII. We hypothesize that the extant NPC evolved early during eukaryotic evolution from a rudimentary structure composed of several identical copies of a few ancestral elements, later diversified and specified by gene duplication. PubMed: 19674973DOI: 10.1074/jbc.M109.023580 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.2 Å) |
Structure validation
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