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Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway.
Biosci Rep. 2018 02 28; 38(1)BR

Abstract

2-C-Methyl-d-erythritol 2,4-cyclodiphosphate synthase (IspF) is a key enzyme in the 2-C-Methyl-d-erythritol-4-phosphate (MEP) pathway of isoprenoid biosynthesis. This enzyme catalyzes the 4-diphosphocytidyl-2-C-methyl-d-erythritol 2-phosphate (CDPME2P) to 2-C-methyl-d-erythritol 2,4-cyclodiphosphate (MEcDP) with concomitant release of cytidine 5'-diphospate (CMP). Bacillus subtilis is a potential host cell for the production of isoprenoids, but few studies are performed on the key enzymes of MEP pathway in B. subtilis In this work, the high-resolution crystal structures of IspF in native and complex with CMP from B. subtilis have been determined. Structural comparisons indicate that there is a looser packing of the subunits of IspF in B. subtilis, whereas the solvent accessible surface of its active pockets is smaller than that in Escherichia coli. Meanwhile, the protein-protein associations of 2-C-Methyl-d-erythritol-4-phosphatecytidyltransferase (IspD), CDPME kinase (IspE) and IspF from B. subtilis and E. coli, which catalyze three consecutive steps in the MEP pathway, are analyzed by native gel shift and size exclusion chromatography methods. The data here show that protein complex assembly is not detectable. These results will be useful for isoprenoid biosynthesis by metabolic engineering.

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Authors+Show Affiliations

Liu Z
Key Laboratory of Environmental and Applied Microbiology, Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu 610041, China. Key Laboratory of Environmental Microbiology of Sichuan Province, Chengdu 610041, China.
Jin Y
Key Laboratory of Environmental and Applied Microbiology, Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu 610041, China. Key Laboratory of Environmental Microbiology of Sichuan Province, Chengdu 610041, China. University of Chinese Academy of Sciences, Beijing 100049, China.
Liu W
Chinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Tao Y
Chinese Academy of Sciences Key Laboratory of Microbial Physiological and Metabolic Engineering, Institute of Microbiology, Chinese Academy of Sciences, Beijing 100101, China.
Wang G
Key Laboratory of Environmental and Applied Microbiology, Chengdu Institute of Biology, Chinese Academy of Sciences, Chengdu 610041, China wanggg@cib.ac.cn. Key Laboratory of Environmental Microbiology of Sichuan Province, Chengdu 610041, China.

MeSH

Aldose-Ketose IsomerasesBacillus subtilisBacterial ProteinsCrystallography, X-RayCytidine DiphosphateErythritolEscherichia coli ProteinsHydrophobic and Hydrophilic InteractionsMetabolic EngineeringMolecular StructurePhosphorus-Oxygen LyasesPhosphotransferases (Alcohol Group Acceptor)Sugar PhosphatesTerpenes

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

29335298

Citation

Liu, Zhongchuan, et al. "Crystal Structure of IspF From Bacillus Subtilis and Absence of Protein Complex Assembly Amongst IspD/IspE/IspF Enzymes in the MEP Pathway." Bioscience Reports, vol. 38, no. 1, 2018.
Liu Z, Jin Y, Liu W, et al. Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway. Biosci Rep. 2018;38(1).
Liu, Z., Jin, Y., Liu, W., Tao, Y., & Wang, G. (2018). Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway. Bioscience Reports, 38(1). https://doi.org/10.1042/BSR20171370
Liu Z, et al. Crystal Structure of IspF From Bacillus Subtilis and Absence of Protein Complex Assembly Amongst IspD/IspE/IspF Enzymes in the MEP Pathway. Biosci Rep. 2018 02 28;38(1) PubMed PMID: 29335298.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway. AU - Liu,Zhongchuan, AU - Jin,Yun, AU - Liu,Weifeng, AU - Tao,Yong, AU - Wang,Ganggang, Y1 - 2018/02/21/ PY - 2017/10/12/received PY - 2018/01/11/revised PY - 2018/01/13/accepted PY - 2018/1/18/pubmed PY - 2018/12/13/medline PY - 2018/1/17/entrez KW - 2-C-methyl-D-erythritol 2 KW - 4-cyclodiphosphate synthase KW - MEP pathway KW - crystal structure KW - isoprenoid biosynthesis JF - Bioscience reports JO - Biosci Rep VL - 38 IS - 1 N2 - 2-C-Methyl-d-erythritol 2,4-cyclodiphosphate synthase (IspF) is a key enzyme in the 2-C-Methyl-d-erythritol-4-phosphate (MEP) pathway of isoprenoid biosynthesis. This enzyme catalyzes the 4-diphosphocytidyl-2-C-methyl-d-erythritol 2-phosphate (CDPME2P) to 2-C-methyl-d-erythritol 2,4-cyclodiphosphate (MEcDP) with concomitant release of cytidine 5'-diphospate (CMP). Bacillus subtilis is a potential host cell for the production of isoprenoids, but few studies are performed on the key enzymes of MEP pathway in B. subtilis In this work, the high-resolution crystal structures of IspF in native and complex with CMP from B. subtilis have been determined. Structural comparisons indicate that there is a looser packing of the subunits of IspF in B. subtilis, whereas the solvent accessible surface of its active pockets is smaller than that in Escherichia coli. Meanwhile, the protein-protein associations of 2-C-Methyl-d-erythritol-4-phosphatecytidyltransferase (IspD), CDPME kinase (IspE) and IspF from B. subtilis and E. coli, which catalyze three consecutive steps in the MEP pathway, are analyzed by native gel shift and size exclusion chromatography methods. The data here show that protein complex assembly is not detectable. These results will be useful for isoprenoid biosynthesis by metabolic engineering. SN - 1573-4935 UR - https://www.unboundmedicine.com/medline/citation/29335298/Crystal_structure_of_IspF_from_Bacillus_subtilis_and_absence_of_protein_complex_assembly_amongst_IspD/IspE/IspF_enzymes_in_the_MEP_pathway_ DB - PRIME DP - Unbound Medicine ER -