Structural highlights
Function
A0A1D8PMH8_CANAL
Publication Abstract from PubMed
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.
Crystal structure of glutamate dehydrogenase 3 from Candida albicans.,Li N, Wang W, Zeng X, Liu M, Li M, Li C, Wang M Biochem Biophys Res Commun. 2021 Jul 13;570:15-20. doi:, 10.1016/j.bbrc.2021.07.014. PMID:34271431[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ 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. 2021 Jul 13;570:15-20. doi:, 10.1016/j.bbrc.2021.07.014. PMID:34271431 doi:http://dx.doi.org/10.1016/j.bbrc.2021.07.014
