3I4R
Nup107(aa658-925)/Nup133(aa517-1156) complex, H.sapiens
Summary for 3I4R
Entry DOI | 10.2210/pdb3i4r/pdb |
Descriptor | Nuclear pore complex protein Nup107, Nuclear pore complex protein Nup133 (2 entities in total) |
Functional Keywords | protein transport, structural protein, kinetochore, mrna transport, nuclear pore complex, nucleus, phosphoprotein, translocation, transport, polymorphism |
Biological source | Homo sapiens (human) More |
Cellular location | Nucleus, nuclear pore complex: P57740 Q8WUM0 |
Total number of polymer chains | 2 |
Total formula weight | 106086.68 |
Authors | Whittle, J.R.R.,Schwartz, T.U. (deposition date: 2009-07-02, 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 (3.53 Å) |
Structure validation
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