Institutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, Anhui, China.
Institutes of Physical Science and Information Technology, Anhui University, Hefei, 230601, Anhui, China; School of Life Sciences, Anhui University, Hefei, 230601, Anhui, China.
Biochem Biophys Res Commun. 2021 Sep 17;570:15-20. doi: 10.1016/j.bbrc.2021.07.014. Epub 2021 Jul 13.
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.
白色念珠菌谷氨酸脱氢酶 3（CaGdh3）催化 l-谷氨酸的可逆氧化脱氨反应，在白色念珠菌的酵母-菌丝过渡中发挥重要作用。本文报道了 CaGdh3 及其与 α-酮戊二酸和 NADPH 复合物的晶体结构。CaGdh3 以六聚体形式存在，每个亚基包含两个结构域。底物和辅酶结合在两个结构域之间的裂隙中，它们的结合诱导 CaGdh3 发生构象变化。本研究结果将有助于理解 CaGdh3 的催化机制，并为靶向 CaGdh3 途径的抗真菌药物设计提供结构基础。
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