7F77

Crystal structure of glutamate dehydrogenase 3 from Candida albicans

Summary for 7F77

• Entry DOI: 10.2210/pdb7f77/pdb
• Descriptor: Glutamate dehydrogenase (2 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: 3
• Total formula weight: 158617.52

Authors

Li, N.,Wang, W.,Zeng, X.,Liu, M.,Li, M.,Li, C.,Wang, M. (deposition date: 2021-06-28, release date: 2021-07-21, Last modification date: 2023-11-29)

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

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: 34271431
DOI: 10.1016/j.bbrc.2021.07.014

Experimental method

X-RAY DIFFRACTION (3.086 Å)