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8QHP

Cysteine tRNA ligase homodimer

Summary for 8QHP
Entry DOI10.2210/pdb8qhp/pdb
EMDB information18415
DescriptorCysteine--tRNA ligase, ZINC ION (2 entities in total)
Functional Keywordscysteine, trna, ligase, synthetase, homodimer, rna
Biological sourcePyrococcus furiosus DSM 3638
Total number of polymer chains2
Total formula weight115248.03
Authors
Pacesa, M.,Correia, B.E.,Levy, E.D. (deposition date: 2023-09-08, release date: 2023-11-29, Last modification date: 2024-02-28)
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
ELECTRON MICROSCOPY (2.8 Å)
Structure validation

227111

数据于2024-11-06公开中

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