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Structure paper

TitleMolecular architecture of OXGR1 reveals an evolutionary conserved mechanisms for metabolite surveillance.
Journal, issue, pagesEMBO J, Year 2026
Publish dateJun 3, 2026
AuthorsXinyue Zhang / Yujie Lu / Xinheng He / Shimeng Guo / Changyao Li / Yu Wang / Yuan Gao / Juxia Yao / Qingning Yuan / Yinshan Tang / Jing Hu / Wen Hu / Zijuan Luo / Kai Wu / Yue Wang / Wanchao Yin / Xin Xie / H Eric Xu / Heng Liu /
PubMed AbstractThe ability of cells to sense and respond to metabolic signals is fundamental to life, yet the molecular mechanisms underlying metabolite surveillance remain incompletely understood. Here, we ...The ability of cells to sense and respond to metabolic signals is fundamental to life, yet the molecular mechanisms underlying metabolite surveillance remain incompletely understood. Here, we elucidate the structural basis of metabolite recognition by OXGR1, a G Protein-Coupled Receptor (GPCR) that senses key intermediates in the tricarboxylic acid (TCA) cycle. Using cryo-electron microscopy, we determined cryo-EM structures of OXGR1 bound to α-ketoglutarate (AKG), itaconate (ITA), and structurally related metabolites succinate (SUC) and maleate (MA). These structures reveal a positively charged binding pocket and an extensive hydrogen-bond network that mediate selective recognition of dicarboxylic acids. In addition, we identify a distinct arrangement of hydrophobic residues that modulates ligand potency and selectivity. Mutational analysis and molecular dynamics simulations further demonstrate that noncanonical micro-switch motifs, including FRY and NLxxY, are essential for ligand recognition and receptor activation. Comparative structural and evolutionary analyses indicate that these mechanisms are conserved across species, underscoring the critical role of OXGR1 in maintaining metabolic homeostasis. Together, our findings define a mechanistic framework for metabolite sensing by OXGR1 and provide a framework for therapeutic modulation of metabolic and inflammatory diseases.
External linksEMBO J / PubMed:42236546
MethodsEM (single particle)
Resolution2.64 - 2.97 Å
Structure data

63580

9m1r

EMDB-63580, PDB-9m1r:
Cryo-EM structure of AKG bound OXGR1-Gq complex
Method: EM (single particle) / Resolution: 2.66 Å

63581

9m1s

EMDB-63581, PDB-9m1s:
Cryo-EM structure of Itaconic acid bound OXGR1-Gq complex
Method: EM (single particle) / Resolution: 2.65 Å

63583

9m1u

EMDB-63583, PDB-9m1u:
Cryo-EM structure of Succinic Acid bound OXGR1-Gq complex
Method: EM (single particle) / Resolution: 2.64 Å

64587

9uxn

EMDB-64587, PDB-9uxn:
Local refinement of Succinate bound OXGR1
Method: EM (single particle) / Resolution: 2.7 Å

64588

9uxo

EMDB-64588, PDB-9uxo:
Local refinement of maleic acid bound OXGR1
Method: EM (single particle) / Resolution: 2.97 Å

64589

9uxp

EMDB-64589, PDB-9uxp:
Local refinement of ITA bound OXGR1
Method: EM (single particle) / Resolution: 2.9 Å

64590

9uxq

EMDB-64590, PDB-9uxq:
Local refinement of AKG bound OXGR1
Method: EM (single particle) / Resolution: 2.89 Å

80947

26xh

EMDB-80947, PDB-26xh:
Cryo-EM structure of Maleic Acid bound OXGR1-Gq complex
Method: EM (single particle) / Resolution: 2.82 Å

Chemicals

ChemComp-MAE:
MALEIC ACID

ChemComp-AKG:
2-OXOGLUTARIC ACID

ChemComp-ITN:
2-methylidenebutanedioic acid

ChemComp-SIN:
SUCCINIC ACID

ChemComp-HOH:
WATER

Source
  • homo sapiens (human)
  • mus musculus (house mouse)
  • lama glama (llama)
KeywordsMEMBRANE PROTEIN/IMMUNE SYSTEM / GPR99 / OXGR1 / Maleic Acid / GPCR / MEMBRANE PROTEIN-IMMUNE SYSTEM complex / MEMBRANE PROTEIN / 2-ketoglutarate; AKG; OXGR1; cryo-EM / Itaconic acid; ITA; OXGR1; cryo-EM / Succinic Acid; OXGR1; cryo-EM / SIGNALING PROTEIN / 2-oxoglutarate / AKG / 2-oxoglutarate receptor 1 / cryo-EM / MA / Itaconate acid / ITA

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