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8Q70

tRNA pseudouridine synthase A homodimer

Summary for 8Q70
Entry DOI10.2210/pdb8q70/pdb
DescriptortRNA pseudouridine synthase A, MAGNESIUM ION, CHLORIDE ION, ... (4 entities in total)
Functional Keywordspseudouridine, synthase, homodimer, pyrococcus, trna, isomerase
Biological sourcePyrococcus furiosus
Total number of polymer chains1
Total formula weight32237.78
Authors
Pacesa, M.,Correia, B.E.,Levy, E.D. (deposition date: 2023-08-15, release date: 2023-11-29, Last modification date: 2024-10-16)
Primary citationSchweke, 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: 38325366
DOI: 10.1016/j.cell.2024.01.022
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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