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KMID : 0624620160490120681
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BMB Reports
2016 Volume.49 No. 12 p.681 ~ p.686
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Crystallographic snapshots of active site metal shift in E. coli fructose 1,6-bisphosphate aldolase
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Tran Huyen-Thi
Lee Seon-Hwa
Ho Thien-Hoang
Hong Seung-Hye
Huynh Kim-Hung
Ahn Yeh-Jin
Oh Deok-Kun
Kang Lin-Woo
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Abstract
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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 A and 2.0 A. 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.
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KEYWORD
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Class II fructose 1,6-bisphosphate aldolase, Inorganic cofactor, Metal ion, X-ray crystallography
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