Crystal structure of glutamate dehydrogenase 3 from Candida albicans

作者：Li, Na; Wang, Wenfeng; Zeng, Xue; Liu, Mingjie; Li, Mengyu; Li, Changrun^*; Wang, Mingzhu^*

来源：Biochemical and Biophysical Research Communications, 2021, 570: 15-20.

DOI：10.1016/j.bbrc.2021.07.014

• Candida albicans
• Yeast-to-hyphal transition
• Glutamate dehydrogenase
• Crystal structure
• Conformational change

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 alpha-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.

• 单位
  安徽大学