Crystal structure of glutamate dehydrogenase 3 from Candida albicans

被引：1

作者：

Li, Na ^{[1
]}

Wang, Wenfeng ^{[1
,2
]}

Zeng, Xue ^{[1
]}

Liu, Mingjie ^{[1
,2
,3
]}

Li, Mengyu ^{[1
,2
,3
]}

Li, Changrun ^{[1
]}

Wang, Mingzhu ^{[1
,2
,3
]}

机构：

[1] Anhui Univ, Inst Phys Sci & Informat Technol, Hefei 230601, Anhui, Peoples R China

[2] Anhui Univ, Sch Life Sci, Hefei 230601, Anhui, Peoples R China

[3] Anhui Univ, Anhui Higher Educ Inst, Key Lab Human Microenvironm & Precis Med, Hefei 230601, Anhui, Peoples R China

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2021年 / 570卷

关键词：

Candida albicans; Yeast-to-hyphal transition; Glutamate dehydrogenase; Crystal structure; Conformational change; SACCHAROMYCES-CEREVISIAE; PLASTICITY; STATES; MODEL;

D O I：

10.1016/j.bbrc.2021.07.014

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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. (C) 2021 Elsevier Inc. All rights reserved.

引用

页码：15 / 20

页数：6

共 32 条

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