Summary for 7N85
| Entry DOI | 10.2210/pdb7n85/pdb |
| Related | 7N84 7N9F |
| EMDB information | 24224 24225 24231 24232 24258 |
| Descriptor | Nucleoporin NUP170, Nucleoporin NUP53, Nucleoporin ASM4, ... (11 entities in total) |
| Functional Keywords | nuclear pore complex, inner ring, spoke, translocase |
| Biological source | Saccharomyces cerevisiae (Baker's yeast) More |
| Total number of polymer chains | 30 |
| Total formula weight | 2801651.10 |
| Authors | Akey, C.W.,Rout, M.P.,Ouch, C.,Echevarria, I.,Fernandez-Martinez, J.,Nudelman, I. (deposition date: 2021-06-13, release date: 2022-01-26, Last modification date: 2024-06-05) |
| Primary citation | Akey, C.W.,Singh, D.,Ouch, C.,Echeverria, I.,Nudelman, I.,Varberg, J.M.,Yu, Z.,Fang, F.,Shi, Y.,Wang, J.,Salzberg, D.,Song, K.,Xu, C.,Gumbart, J.C.,Suslov, S.,Unruh, J.,Jaspersen, S.L.,Chait, B.T.,Sali, A.,Fernandez-Martinez, J.,Ludtke, S.J.,Villa, E.,Rout, M.P. Comprehensive structure and functional adaptations of the yeast nuclear pore complex. Cell, 185:361-378.e25, 2022 Cited by PubMed Abstract: Nuclear pore complexes (NPCs) mediate the nucleocytoplasmic transport of macromolecules. Here we provide a structure of the isolated yeast NPC in which the inner ring is resolved by cryo-EM at sub-nanometer resolution to show how flexible connectors tie together different structural and functional layers. These connectors may be targets for phosphorylation and regulated disassembly in cells with an open mitosis. Moreover, some nucleoporin pairs and transport factors have similar interaction motifs, which suggests an evolutionary and mechanistic link between assembly and transport. We provide evidence for three major NPC variants that may foreshadow functional specializations at the nuclear periphery. Cryo-electron tomography extended these studies, providing a model of the in situ NPC with a radially expanded inner ring. Our comprehensive model reveals features of the nuclear basket and central transporter, suggests a role for the lumenal Pom152 ring in restricting dilation, and highlights structural plasticity that may be required for transport. PubMed: 34982960DOI: 10.1016/j.cell.2021.12.015 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (7.6 Å) |
Structure validation
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