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Structure paper

TitleStructural Mechanism of Filamentation Induced Dampening of GTP Inhibition of Glutamate Dehydrogenase.
Journal, issue, pagesbioRxiv, Year 2026
Publish dateJul 7, 2026
AuthorsZelin Shan / Noura I Darwish / Andres Rivero-Gamez / Timothy S Strutzenberg / Dmitry Lyumkis / Nancy C Horton /
PubMed AbstractGlutamate dehydrogenase (GDH) is a highly regulated key enzyme that catalyzes the reversible oxidative deamination of glutamate to -ketoglutarate, positioning it at a critical hub linking amino acid ...Glutamate dehydrogenase (GDH) is a highly regulated key enzyme that catalyzes the reversible oxidative deamination of glutamate to -ketoglutarate, positioning it at a critical hub linking amino acid catabolism to energy production while supplying ammonia for urea synthesis and other nitrogen pathways. Early investigations have shown that bovine GDH (bGDH), which shares 98% sequence identity with its human homolog, assembles into polymeric filaments with altered allosteric responses. Filamentation has only relatively recently been appreciated as a widespread mechanism of enzyme regulation, prompting a reevaluation of these early observations in GDH. Here, we use high-resolution cryogenic electron microscopy (cryo-EM) to show that bGDH hexamers assemble via reciprocal "antenna" interactions that oppose the conformational changes associated with GTP inhibition, revealing how filamentation reshapes GDH allostery and with implications for the treatment of human disease.
External linksbioRxiv / PubMed:42465363 / PubMed Central
MethodsEM (single particle)
Resolution2.18 - 3.52 Å
Structure data

EMDB-74574: Consensus map of the bGDH di-hexamer in apo form
Method: EM (single particle) / Resolution: 2.55 Å

EMDB-74575: Constituent map A of the bGDH di-hexamer in apo form
Method: EM (single particle) / Resolution: 2.89 Å

74576

9zqr

EMDB-74576, PDB-9zqr:
Composite map of the bGDH di-hexamer in apo form
Method: EM (single particle) / Resolution: 2.9 Å

74577

9zqs

EMDB-74577, PDB-9zqs:
Mono-hexameric bGDH map in apo form
Method: EM (single particle) / Resolution: 2.52 Å

EMDB-74578: Consensus map of the bGDH di-hexamer in liganded form
Method: EM (single particle) / Resolution: 3.44 Å

EMDB-74579: Constituent map A of the bGDH di-hexamer in liganded form
Method: EM (single particle) / Resolution: 3.52 Å

EMDB-74580: Constituent map B of the bGDH di-hexamer in liganded form
Method: EM (single particle) / Resolution: 3.29 Å

74581

9zqt

EMDB-74581, PDB-9zqt:
Composite map of the bGDH di-hexamer in liganded form
Method: EM (single particle) / Resolution: 3.5 Å

74582

9zqu

EMDB-74582, PDB-9zqu:
Mono-hexameric bGDH map in liganded form
Method: EM (single particle) / Resolution: 2.18 Å

Chemicals

ChemComp-HOH:
WATER

ChemComp-GTP:
GUANOSINE-5'-TRIPHOSPHATE / GTP, energy-carrying molecule*YM

ChemComp-NAI:
1,4-DIHYDRONICOTINAMIDE ADENINE DINUCLEOTIDE

ChemComp-GGL:
GAMMA-L-GLUTAMIC ACID

Source
  • Bos taurus (Bovine) (domestic cattle)
  • bos taurus (domestic cattle)
KeywordsUNKNOWN FUNCTION / Glutamate dehydrogenase Amino acid metabolism filament allosteric regulation

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