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大肠杆菌1,6-二磷酸果糖醛缩酶活性位点金属离子移位的晶体学快照。

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

作者信息

Tran Huyen-Thi, Lee Seon-Hwa, Ho Thien-Hoang, Hong Seung-Hye, Huynh Kim-Hung, Ahn Yeh-Jin, Oh Deok-Kun, Kang Lin-Woo

机构信息

Department of Biological Sciences, Konkuk University, Seoul 05029, Korea; 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.

Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Korea.

出版信息

BMB Rep. 2016 Dec;49(12):681-686. doi: 10.5483/bmbrep.2016.49.12.132.

DOI:10.5483/bmbrep.2016.49.12.132
PMID:27733232
原文链接:https://pmc.ncbi.nlm.nih.gov/articles/PMC5346313/
Abstract

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. [BMB Reports 2016; 49(12): 681-686].

摘要

1,6-二磷酸果糖醛缩酶（FBA）在生命过程中的糖酵解和糖异生作用中都很重要。II类（锌依赖性）FBA是开发抗原生动物、细菌和真菌抗生素的一个有吸引力的靶点，并且在化学和制药工业中也被广泛用于生产各种高价值的立体异构体。在本研究中，从四种不同晶体中测定了II类大肠杆菌FBA（EcFBA）的晶体结构，分辨率在1.8 Å至2.0 Å之间。天然EcFBA结构显示了Zn2＋离子的两个独立位点，即Zn1（内部位置）和Zn2（活性位点表面位置）。柠檬酸和TRIS结合的EcFBA结构显示Zn2＋仅位于Zn2位置。有配体结合和无配体结合的EcFBA结构的晶体学快照提出了活性位点处金属移位的原理，这可能是一种将微量金属辅因子Zn2＋保留在EcFBA内而不丢失的隐藏机制。[《BMB报告》2016年；49(12): 681 - 686]

https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/f607cea23a0b/bmb-49-681f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/db363b01083c/bmb-49-681f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/d55aaefda3aa/bmb-49-681f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/d38b8f3abc2b/bmb-49-681f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/f607cea23a0b/bmb-49-681f4.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/db363b01083c/bmb-49-681f1.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/d55aaefda3aa/bmb-49-681f2.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/d38b8f3abc2b/bmb-49-681f3.jpg
https://cdn.ncbi.nlm.nih.gov/pmc/blobs/0b26/5346313/f607cea23a0b/bmb-49-681f4.jpg

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