8QHP

Cysteine tRNA ligase homodimer

8QHP の概要

• エントリーDOI: 10.2210/pdb8qhp/pdb
• EMDBエントリー: 18415
• 分子名称: Cysteine--tRNA ligase, ZINC ION (2 entities in total)
• 機能のキーワード: cysteine, trna, ligase, synthetase, homodimer, rna
• 由来する生物種: Pyrococcus furiosus DSM 3638
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 115248.03

構造登録者

Pacesa, M.,Correia, B.E.,Levy, E.D. (登録日: 2023-09-08, 公開日: 2023-11-29, 最終更新日: 2024-02-28)

主引用文献

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

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

実験手法

ELECTRON MICROSCOPY (2.8 Å)