8P49
Uncharacterized Q8U0N8 protein from Pyrococcus furiosus
Summary for 8P49
| Entry DOI | 10.2210/pdb8p49/pdb |
| EMDB information | 17402 |
| Descriptor | Q8U0N8 protein (1 entity in total) |
| Functional Keywords | uncharacterized, hexamer, pyrococcus, pore, unknown function |
| Biological source | Pyrococcus furiosus DSM 3638 |
| Total number of polymer chains | 6 |
| Total formula weight | 280404.77 |
| Authors | Pacesa, M.,Correia, B.E.,Levy, E.D. (deposition date: 2023-05-19, release date: 2023-11-29, Last modification date: 2024-02-28) |
| Primary citation | Schweke, H.,Pacesa, M.,Levin, T.,Goverde, C.A.,Kumar, P.,Duhoo, Y.,Dornfeld, L.J.,Dubreuil, B.,Georgeon, S.,Ovchinnikov, S.,Woolfson, D.N.,Correia, B.E.,Dey, S.,Levy, E.D. An atlas of protein homo-oligomerization across domains of life. Cell, 187:999-, 2024 Cited by PubMed Abstract: Protein structures are essential to understanding cellular processes in molecular detail. While advances in artificial intelligence revealed the tertiary structure of proteins at scale, their quaternary structure remains mostly unknown. We devise a scalable strategy based on AlphaFold2 to predict homo-oligomeric assemblies across four proteomes spanning the tree of life. Our results suggest that approximately 45% of an archaeal proteome and a bacterial proteome and 20% of two eukaryotic proteomes form homomers. Our predictions accurately capture protein homo-oligomerization, recapitulate megadalton complexes, and unveil hundreds of homo-oligomer types, including three confirmed experimentally by structure determination. Integrating these datasets with omics information suggests that a majority of known protein complexes are symmetric. Finally, these datasets provide a structural context for interpreting disease mutations and reveal coiled-coil regions as major enablers of quaternary structure evolution in human. Our strategy is applicable to any organism and provides a comprehensive view of homo-oligomerization in proteomes. PubMed: 38325366DOI: 10.1016/j.cell.2024.01.022 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.79 Å) |
Structure validation
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