Structural insights into the committed step of bacterial phospholipid biosynthesis

doi:10.1038/s41467-017-01821-9

KMS > iHuman研究所 > 特聘教授组 > Raymond Stevens组

	Structural insights into the committed step of bacterial phospholipid biosynthesis
	Li, Zhenjian 1; Tang, Yannan 1,2,3; Wu, Yiran3 ; Zhao, Suwen4 ; Bao, Juan 1; Luo, Yitian1,2,4 ; Li, Dianfan 1
	2017-11-22
发表期刊	NATURE COMMUNICATIONS (IF:14.7[JCR-2023],16.1[5-Year])
ISSN	2041-1723
卷号	8
发表状态	已发表
DOI	10.1038/s41467-017-01821-9
摘要	The membrane-integral glycerol 3-phosphate (G3P) acyltransferase PlsY catalyses the committed and essential step in bacterial phospholipid biosynthesis by acylation of G3P, forming lysophosphatidic acid. It contains no known acyltransferase motifs, lacks eukaryotic homologs, and uses the unusual acyl-phosphate as acyl donor, as opposed to acyl-CoA or acyl-carrier protein for other acyltransferases. Previous studies have identified several PlsY inhibitors as potential antimicrobials. Here we determine the crystal structure of PlsY at 1.48 angstrom resolution, revealing a seven-transmembrane helix fold. Four additional substrate-and product-bound structures uncover the atomic details of its relatively inflexible active site. Structure and mutagenesis suggest a different acylation mechanism of 'substrate-assisted catalysis' that, unlike other acyltransferases, does not require a proteinaceous catalytic base to complete. The structure data and a high-throughput enzymatic assay developed in this work should prove useful for virtual and experimental screening of inhibitors against this vital bacterial enzyme.
收录类别	SCI
语种	英语
资助项目	Key Program of CAS Frontier Science[QYZDB-SSW-SMC037]
WOS研究方向	Science & Technology - Other Topics
WOS类目	Multidisciplinary Sciences
WOS记录号	WOS:000416226200020
出版者	NATURE PUBLISHING GROUP
WOS关键词	LIPID CUBIC PHASE ; CRYSTAL-STRUCTURE ; MEMBRANE-PROTEINS ; ACID SYNTHESIS ; ACTIVE-SITE ; ACYLTRANSFERASE ; TARGET ; PLSY ; CRYSTALLOGRAPHY ; CHEMISTRY
原始文献类型	Article
引用统计	正在获取...
文献类型	期刊论文
条目标识符	https://kms.shanghaitech.edu.cn/handle/2MSLDSTB/14300
专题	iHuman研究所_特聘教授组_Raymond Stevens组生命科学与技术学院 iHuman研究所_PI研究组_赵素文组生命科学与技术学院_硕士生生命科学与技术学院_博士生
通讯作者	Li, Dianfan
作者单位	1.Chinese Acad Sci, Shanghai Inst Biochem & Cell Biol, Ctr Excellence Mol Cell Sci, Natl Ctr Prot Sci Shanghai,State Key Lab Mol Biol, 333 Haike Rd, Shanghai 201210, Peoples R China 2.Univ Chinese Acad Sci, Shanghai 201210, Peoples R China 3.ShanghaiTech Univ, iHuman Inst, 333 Middle Huaxia Rd, Shanghai 201210, Peoples R China 4.ShanghaiTech Univ, Sch Life Sci & Technol, 333 Middle Huaxia Rd, Shanghai 201210, Peoples R China
推荐引用方式 GB/T 7714	Li, Zhenjian,Tang, Yannan,Wu, Yiran,et al. Structural insights into the committed step of bacterial phospholipid biosynthesis[J]. NATURE COMMUNICATIONS,2017,8.
APA	Li, Zhenjian.,Tang, Yannan.,Wu, Yiran.,Zhao, Suwen.,Bao, Juan.,...&Li, Dianfan.(2017).Structural insights into the committed step of bacterial phospholipid biosynthesis.NATURE COMMUNICATIONS,8.
MLA	Li, Zhenjian,et al."Structural insights into the committed step of bacterial phospholipid biosynthesis".NATURE COMMUNICATIONS 8(2017).