生物
蛋白质组
四级结构
背景(考古学)
进化生物学
蛋白质结构
三域系统
计算生物学
遗传学
基因组
生物化学
基因
古生物学
蛋白质亚单位
作者
Shoshana J. Wodak,Martin Pačesa,Tal Levin,Casper Goverde,Prasun Kumar,Yoan Duhoo,Leslie Dornfeld,Benjamin Dubreuil,Sandrine Georgeon,С. Г. Овчинников,Derek N. Woolfson,Bruno E. Correia,Sucharita Dey,Emmanuel D. Levy
出处
期刊:Cell
[Elsevier]
日期:2024-02-01
卷期号:187 (4): 999-1010.e15
被引量:1
标识
DOI:10.1016/j.cell.2024.01.022
摘要
Summary
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.
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