Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway

doi:10.1042/BSR20171370

CORC > 成都生物研究所 > 中国科学院成都生物研究所 > 食品安全与环境治理领域 > 应用与环境微生物研究

	Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway
	Liu, Zhongchuan 1,2; Jin, Yun 1,2,4; Liu, Weifeng 3; Tao, Yong 3; Wang, Ganggang 1,2
刊名	BIOSCIENCE REPORTS
	2018
卷号	38 页码:BSR20171370
ISSN号	0144-8463
DOI	10.1042/BSR20171370
产权排序	1
文献子类	Article
英文摘要	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.
URL标识	查看原文
WOS关键词	NON-MEVALONATE PATHWAY ; COLI 2C-METHYL-D-ERYTHRITOL-2,4-CYCLODIPHOSPHATE SYNTHASE ; METHYLERYTHRITOL PHOSPHATE-PATHWAY ; ISOPRENOID PRECURSOR PATHWAY ; 2,4-CYCLODIPHOSPHATE SYNTHASE ; ARABIDOPSIS-THALIANA ; SEQUENCE ALIGNMENT ; BIOSYNTHESIS ; INHIBITORS ; BACTERIA
WOS研究方向	Biochemistry & Molecular Biology ; Cell Biology
语种	英语
出版者	PORTLAND PRESS LTD
WOS记录号	WOS:000462677200004
内容类型	期刊论文
源URL	[http://210.75.237.14/handle/351003/30854]
专题	环境治理与食品安全领域_应用与环境微生物研究
作者单位	1.Chinese Acad Sci, Chengdu Inst Biol, Key Lab Environm & Appl Microbiol, Chengdu 610041, Sichuan, Peoples R China; 2.Key Lab Environm Microbiol Sichuan Prov, Chengdu 610041, Sichuan, Peoples R China; 3.Chinese Acad Sci, Inst Microbiol, Key Lab Microbial Physiol & Metab Engn, Beijing 100101, Peoples R China; 4.Univ Chinese Acad Sci, Beijing 100049, Peoples R China
推荐引用方式 GB/T 7714	Liu, Zhongchuan,Jin, Yun,Liu, Weifeng,et al. Crystal structure of IspF from Bacillus subtilis and absence of protein complex assembly amongst IspD/IspE/IspF enzymes in the MEP pathway[J]. BIOSCIENCE REPORTS,2018,38:BSR20171370.
APA	Liu, Zhongchuan,Jin, Yun,Liu, Weifeng,Tao, Yong,&Wang, Ganggang.(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,BSR20171370.
MLA	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 38(2018):BSR20171370.