Summary for 8TJ5
| Entry DOI | 10.2210/pdb8tj5/pdb |
| Related | 8T9L 8TIE |
| EMDB information | 41114 41116 41117 41119 41120 41121 41122 41123 41285 41300 |
| Descriptor | Spoke connector, Nucleoporin NUP53, Nucleoporin 59, ... (11 entities in total) |
| Functional Keywords | nuclear pore complex, nucleocytoplasmic transport, nucleoporin, membrane protein, translocase, transport protein |
| Biological source | Saccharomyces cerevisiae More |
| Total number of polymer chains | 46 |
| Total formula weight | 2852491.63 |
| Authors | Akey, C.W.,Echeverria, I.,Ouch, C.,Fernandez-Martinez, J.,Rout, M.P. (deposition date: 2023-07-20, release date: 2023-10-11) |
| Primary citation | Akey, C.W.,Echeverria, I.,Ouch, C.,Nudelman, I.,Shi, Y.,Wang, J.,Chait, B.T.,Sali, A.,Fernandez-Martinez, J.,Rout, M.P. Implications of a multiscale structure of the yeast nuclear pore complex. Mol.Cell, 83:3283-3302.e5, 2023 Cited by PubMed Abstract: Nuclear pore complexes (NPCs) direct the nucleocytoplasmic transport of macromolecules. Here, we provide a composite multiscale structure of the yeast NPC, based on improved 3D density maps from cryogenic electron microscopy and AlphaFold2 models. Key features of the inner and outer rings were integrated into a comprehensive model. We resolved flexible connectors that tie together the core scaffold, along with equatorial transmembrane complexes and a lumenal ring that anchor this channel within the pore membrane. The organization of the nuclear double outer ring reveals an architecture that may be shared with ancestral NPCs. Additional connections between the core scaffold and the central transporter suggest that under certain conditions, a degree of local organization is present at the periphery of the transport machinery. These connectors may couple conformational changes in the scaffold to the central transporter to modulate transport. Collectively, this analysis provides insights into assembly, transport, and NPC evolution. PubMed: 37738963DOI: 10.1016/j.molcel.2023.08.025 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (6.6 Å) |
Structure validation
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