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Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer

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Title
Quantifying structural relationships of metal-binding sites suggests origins of biological electron transfer
Author(s)
Bromberg, Yana; Aptekmann, Ariel A.; Mahlich, Yannick; Linda Cook; Senn, Stefan; Miller, Maximillian; Nanda, Vikas; Ferreiro, Diego U.; Falkowski, Paul G.
Publication Date
2022-01
Journal
Science Advances, v.8, no.2
Publisher
American Association for the Advancement of Science
Abstract
© 2022 The Authors, some rights reserved; exclusive licensee American Association for the Advancement of Science. No claim to original U.S. Government Works. Distributed under a Creative Commons Attribution License 4.0 (CC BY).Biological redox reactions drive planetary biogeochemical cycles. Using a novel, structure-guided sequence analysis of proteins, we explored the patterns of evolution of enzymes responsible for these reactions. Our analysis reveals that the folds that bind transition metal-containing ligands have similar structural geometry and amino acid sequences across the full diversity of proteins. Similarity across 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 peptide origins. We 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.
URI
https://pr.ibs.re.kr/handle/8788114/12965
DOI
10.1126/sciadv.abj3984
ISSN
2375-2548
Appears in Collections:
Pioneer Research Center for Mathematical and Computational Sciences(수리 및 계산과학 연구단) > Discrete Mathematics Group(이산 수학 그룹) > 1. Journal Papers (저널논문)
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