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TitleRepeatability of protein structural evolution following convergent gene fusions.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8278, Year 2025
Publish dateSep 22, 2025
AuthorsNaoki Konno / Keita Miyake / Satoshi Nishino / Kimiho Omae / Haruaki Yanagisawa / Saburo Tsuru / Yuki Nishimura / Masahide Kikkawa / Chikara Furusawa / Wataru Iwasaki /
PubMed AbstractConvergent evolution of proteins provides insights into repeatability of genetic adaptation. While local convergence of proteins at residue or domain level has been characterized, global structural ...Convergent evolution of proteins provides insights into repeatability of genetic adaptation. While local convergence of proteins at residue or domain level has been characterized, global structural convergence by inter-domain/molecular interactions remains largely unknown. Here we present structural convergent evolution on fusion enzymes of aldehyde dehydrogenases (ALDHs) and alcohol dehydrogenases (ADHs). We discover BdhE (bifunctional dehydrogenase E), an enzyme clade that emerged independently from the previously known AdhE family through distinct gene fusion events. AdhE and BdhE show shared enzymatic activities and non-overlapping phylogenetic distribution, suggesting common functions in different species. Cryo-electron microscopy reveals BdhEs form donut-like homotetramers, contrasting AdhE's helical homopolymers. Intriguingly, despite distinct quaternary structures and < 30% amino acid sequence identity, both enzymes forms resemble dimeric structure units by ALDH-ADH interactions via convergently elongated loop structures. These findings suggest convergent gene fusions recurrently led to substrate channeling evolution to enhance two-step reaction efficiency. Our study unveils structural convergence at inter-domain/molecular level, expanding our knowledges on patterns behind molecular evolution exploring protein structural universe.
External linksNat Commun / PubMed:40983608 / PubMed Central
MethodsEM (single particle)
Resolution2.55 - 2.79 Å
Structure data

63003

9ldk

EMDB-63003, PDB-9ldk:
The complex structure of Escherichia coli AdhE (compact conformation)
Method: EM (single particle) / Resolution: 2.79 Å

63004

9ldl

EMDB-63004, PDB-9ldl:
The complex structure of Halomonas eurihalina BdhE
Method: EM (single particle) / Resolution: 2.55 Å

Source
  • escherichia coli k-12 (bacteria)
  • halomonas eurihalina (bacteria)
KeywordsBIOSYNTHETIC PROTEIN / Complex / Enzyme

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