09:40 〜 10:00
[MIS06-03] Metallic signatures of the origins of life
★Invited Papers
Biological redox reactions drive planetary biogeochemical cycles. Using a novel, protein 3D structure-guided analysis, we explored the evolution of redox enzymes.
We found that the protein folds that bind transition metal–containing ligands have similar structural geometry and amino acid sequences across the full diversity of available protein structures.
Patterns in similarity of folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal–ligand binding had a small number of common origins.
We also observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions.
Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.
We found that the protein folds that bind transition metal–containing ligands have similar structural geometry and amino acid sequences across the full diversity of available protein structures.
Patterns in similarity of folds reflects the availability of key transition metals over geological time and strongly suggests that transition metal–ligand binding had a small number of common origins.
We also observe that structures central to our similarity network come primarily from oxidoreductases, suggesting that ancestral peptides may have also facilitated electron transfer reactions.
Last, our results reveal that the earliest biologically functional peptides were likely available before the assembly of fully functional protein domains over 3.8 billion years ago.