8q70
tRNA pseudouridine synthase A homodimer
Structural highlights
FunctionTRUA_PYRFU Formation of pseudouridine at positions 38, 39 and 40 in the anticodon stem and loop of transfer RNAs. Publication Abstract from PubMedProtein 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. An atlas of protein homo-oligomerization across domains of life.,Schweke H, Pacesa M, Levin T, Goverde CA, Kumar P, Duhoo Y, Dornfeld LJ, Dubreuil B, Georgeon S, Ovchinnikov S, Woolfson DN, Correia BE, Dey S, Levy ED Cell. 2024 Feb 15;187(4):999-1010.e15. doi: 10.1016/j.cell.2024.01.022. Epub 2024 , Feb 6. PMID:38325366[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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