Crystallographic snapshots of active site metal shift in E. coli fructose 1,6-bisphosphate aldolase

BMB Reports

Huyen-Thi Tran^1,2¹  Thien-Hoang Ho^1²  Seon-Hwa Lee^3³  Seung-Hye Hong^3⁴ 

[1] Department of Biological Sciences, Konkuk University, Seoul 05029, Korea^1;Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Korea^3;Department of Biotechnology and Food Technology, Industrial University of Ho Chi Minh City, 12 Nguyen Van Bao Street, Ward 4, Go Vap District, Ho Chi Minh City, Vietnam^2;Department of Life Science, Sangmyung University, Seoul 03016, Korea^4

关键词: Class II fructose 1;    6-bisphosphate aldolase;   

DOI  :  10.5483/BMBRep.2016.49.12.132

学科分类：生物化学/生物物理

来源: Korean Society for Biochemistry and Molecular Biology

【 摘 要 】

Fructose 1,6-bisphosphate aldolase (FBA) is important for both glycolysis and gluconeogenesis in life. Class II (zinc dependent) FBA is an attractive target for the development of antibiotics against protozoa, bacteria, and fungi, and is also widely used to produce various high-value stereoisomers in the chemical and pharmaceutical industry. In this study, the crystal structures of class II Escherichia coli FBA (EcFBA) were determined from four different crystals, with resolutions between 1.8 Å and 2.0 Å. Native EcFBA structures showed two separate sites of Zn1 (interior position) and Zn2 (active site surface position) for Zn2+ ion. Citrate and TRIS bound EcFBA structures showed Zn2+ position exclusively at Zn2. Crystallographic snapshots of EcFBA structures with and without ligand binding proposed the rationale of metal shift at the active site, which might be a hidden mechanism to keep the trace metal cofactor Zn2+ within EcFBA without losing it.

【 授权许可】

Unknown