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TitleMulti-domain O-GlcNAcase structures reveal allosteric regulatory mechanisms.
Journal, issue, pagesNat Commun, Vol. 16, Issue 1, Page 8828, Year 2025
Publish dateOct 3, 2025
AuthorsSara Basse Hansen / Sergio G Bartual / Huijie Yuan / Olawale G Raimi / Andrii Gorelik / Andrew T Ferenbach / Kristian Lytje / Jan Skov Pedersen / Taner Drace / Thomas Boesen / Daan M F van Aalten /
PubMed AbstractNucleocytoplasmic protein O-GlcNAcylation is a dynamic modification catalysed by O-GlcNAc transferase (OGT) and reversed by O-GlcNAc hydrolase (OGA), whose activities are regulated through largely ...Nucleocytoplasmic protein O-GlcNAcylation is a dynamic modification catalysed by O-GlcNAc transferase (OGT) and reversed by O-GlcNAc hydrolase (OGA), whose activities are regulated through largely unknown O-GlcNAc-dependent feedback mechanisms. OGA is a homodimeric, multi-domain enzyme containing a catalytic core and a pseudo-histone acetyltransferase (pHAT) domain. While a catalytic structure has been reported, the structure and function of the pHAT domain remain elusive. Here, we report a crystal structure of the Trichoplax adhaerens pHAT domain and cryo-EM data of the multi-domain T. adhaerens and human OGAs, complemented by biophysical analyses. Here, we show that the eukaryotic OGA pHAT domain forms catalytically incompetent, symmetric homodimers, projecting a partially conserved putative peptide-binding site. In solution, OGA exist as flexible multi-domain dimers, but catalytic core-pHAT linker interactions restrict pHAT positional range. In human OGA, pHAT movements remodel the active site environment through conformational changes in a flexible arm region. These findings reveal allosteric mechanisms through which the pHAT domain contributes to O-GlcNAc homeostasis.
External linksNat Commun / PubMed:41044083 / PubMed Central
MethodsEM (single particle)
Resolution2.99 - 3.08 Å
Structure data

53081

9qen

EMDB-53081, PDB-9qen:
Cryo-EM structure of human O-GlcNAcase
Method: EM (single particle) / Resolution: 3.08 Å

53082

9qep

EMDB-53082, PDB-9qep:
Cryo-EM structure of O-GlcNAcase from Trichoplax Adhaerens
Method: EM (single particle) / Resolution: 2.99 Å

Source
  • trichoplax adhaerens (invertebrata)
  • homo sapiens (human)
KeywordsHYDROLASE / GH84 hydrolase

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