7F79
Crystal structure of glutamate dehydrogenase 3 from Candida albicans in complex with alpha-ketoglutarate and NADPH
Summary for 7F79
Entry DOI | 10.2210/pdb7f79/pdb |
Related | 7F77 |
Descriptor | Glutamate dehydrogenase, NADPH DIHYDRO-NICOTINAMIDE-ADENINE-DINUCLEOTIDE PHOSPHATE, 2-OXOGLUTARIC ACID, ... (5 entities in total) |
Functional Keywords | candida albicans, yeast-to-hyphal transition, glutamate dehydrogenase, conformational change, oxidoreductase |
Biological source | Candida albicans SC5314 (Yeast) |
Total number of polymer chains | 6 |
Total formula weight | 323044.63 |
Authors | |
Primary citation | Li, N.,Wang, W.,Zeng, X.,Liu, M.,Li, M.,Li, C.,Wang, M. Crystal structure of glutamate dehydrogenase 3 from Candida albicans. Biochem.Biophys.Res.Commun., 570:15-20, 2021 Cited by PubMed Abstract: Glutamate dehydrogenase 3 from Candida albicans (CaGdh3) catalyzes the reversible oxidative deamination of l-glutamate, playing an important role in the yeast-to-hyphal transition of C. albicans. Here we report the crystal structures of CaGdh3 and its complex with α-ketoglutarate and NADPH. CaGdh3 exists as a hexamer, with each subunit containing two domains. The substrate and coenzyme bind in the cleft between the two domains and their binding induces a conformational change in CaGdh3. Our results will help to understand the catalytic mechanism of CaGdh3 and will provide a structural basis for the design of antifungal drugs targeting the CaGdh3 pathway. PubMed: 34271431DOI: 10.1016/j.bbrc.2021.07.014 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.7 Å) |
Structure validation
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