9ZQS
Mono-hexameric bGDH map in apo form
Summary for 9ZQS
| Entry DOI | 10.2210/pdb9zqs/pdb |
| EMDB information | 74577 |
| Descriptor | Glutamate dehydrogenase 1, mitochondrial (2 entities in total) |
| Functional Keywords | glutamate dehydrogenase amino acid metabolism filament allosteric regulation, unknown function |
| Biological source | Bos taurus (domestic cattle) |
| Total number of polymer chains | 6 |
| Total formula weight | 369562.99 |
| Authors | |
| Primary citation | Shan, Z.,Darwish, N.I.,Rivero-Gamez, A.,Strutzenberg, T.S.,Lyumkis, D.,Horton, N.C. Structural Mechanism of Filamentation Induced Dampening of GTP Inhibition of Glutamate Dehydrogenase. Biorxiv, 2026 Cited by PubMed Abstract: Glutamate dehydrogenase (GDH) is a highly regulated key enzyme that catalyzes the reversible oxidative deamination of glutamate to α-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. PubMed: 42465363DOI: 10.64898/2026.07.06.736867 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.52 Å) |
Structure validation
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