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TitleA repurposed AMP binding domain reveals mitochondrial protein AMPylation as a regulator of cellular metabolism.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 7863, Year 2025
Publish dateAug 23, 2025
AuthorsAbner Gonzalez / Alex Pon / Kelly Servage / Krzysztof Pawłowski / Yan Han / Anju Sreelatha /
PubMed AbstractProtein AMPylation, the covalent addition of adenosine monophosphate (AMP) to protein substrates, has been known as a post translational modification for over 50 years. Research in this field is ...Protein AMPylation, the covalent addition of adenosine monophosphate (AMP) to protein substrates, has been known as a post translational modification for over 50 years. Research in this field is largely underdeveloped due to the lack of tools that enable the systematic identification of AMPylated substrates. Here, we address this gap by developing an enrichment technique to isolate and study AMPylated proteins using a nucleotide-binding protein, hinT. Cryo-EM reconstruction of an AMPylated protein bound to hinT provides a structural basis for AMP selectivity. Using structure guided mutagenesis, we optimize enrichment to identify novel substrates of the evolutionarily conserved AMPylase, Selenoprotein O. We show that mammalian Selenoprotein O regulates metabolic flux through AMPylation of key mitochondrial proteins including glutamate dehydrogenase and pyruvate dehydrogenase. Our findings highlight the broader significance of AMPylation, an emerging post translational modification with critical roles in signal transduction and disease pathology. Furthermore, we establish a powerful enrichment platform for the discovery of novel AMPylated proteins to study the mechanisms and significance of protein AMPylation in cellular function.
External linksNat Commun / PubMed:40849408 / PubMed Central
MethodsEM (single particle)
Resolution2.2 - 2.7 Å
Structure data

42892

8v1y

EMDB-42892, PDB-8v1y:
Composite map of AMPylated GlnA bound to hinT
Method: EM (single particle) / Resolution: 2.7 Å

42896

8v22

EMDB-42896, PDB-8v22:
GlnA dodecamer with AMPylation
Method: EM (single particle) / Resolution: 2.2 Å

Chemicals

ChemComp-AMP:
ADENOSINE MONOPHOSPHATE / AMP*YM

ChemComp-MN:
Unknown entry

Source
  • escherichia coli (E. coli)
KeywordsLIGASE/HYDROLASE / AMPylation / adenyltransferase / nucleotide binding protein / LIGASE-HYDROLASE complex / LIGASE

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