Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase

doi:10.1016/j.ijbiomac.2021.06.107

IOCAS-IR > 实验海洋生物学重点实验室

	Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase
	Wang, Fang 1,2,3; Liu, Changshui 1,2,4; Wang, Chongyang 1,2,3; Wang, Yan 1,2,3; Zang, Kun 1,2,3; Wang, Xin 1,2,3; Liu, Xiaohua 5; Li, Shihao 1,2,3,4; Li, Fuhua 1,2,3,4; Ma, Qingjun 1,2,3,4
	2021-08-01
发表期刊	INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES
ISSN	0141-8130
卷号	184 页码:821-830
通讯作者	Ma, Qingjun(qma@qdio.ac.cn)
摘要	dUTPases are key enzymes in all life kingdoms. A staphylococcal repressor protein (Stl) inhibited dUTPases from multiple species to various extents. Understanding the molecular basis underlying the inhibition differences is crucial to develop effective proteinaceous inhibitors of dUTPases. Herein, we report the complex structure of Stl N-terminal domain (StlN-ter) and Litopenaeus vannamei dUTPase domain (lvDUT65-210). Stl inhibited lvDUT65-210 through its N-terminal domain. The lvDUT65-210-StlN-ter complex structure revealed a heterohexamer encompassing three StlN-ter monomers bound to one lvDUT65-210 trimer, generating two types of Stl-dUTPase interfaces. Interface I is formed by Stl interaction with the lvDUT65-210 active-site region that is contributed by motifs I-IV from its two subunits; interface II results from Stl binding to the C-terminal motif V of the third lvDUT65-210 subunit. Structural comparison revealed both conserved features and obvious differences in Stl-dUTPase interaction patterns, giving clues about the inhibition differences of Stl on dUTPases. Noticeably, interface II is only observed in lvDUT65-210-StlN-ter. The Stl-interacting residues of lvDUT65-210 are conserved in other eukaryotic dUTPases, particularly human dUTPase. Altogether, our study presents the first structural model of Stl interaction with eukaryotic dUTPase, contributing to a more complete view of Stl inhibition and facilitating the development of proteinaceous inhibitor for eukaryotic dUTPases.
关键词	Stl dUTPase interactions Proteinaceous inhibitor Crystal structure
DOI	10.1016/j.ijbiomac.2021.06.107
收录类别	SCI
语种	英语
资助项目	National Natural Science Foundation of China[31572660] ; National Natural Science Foundation of China[31872600] ; Qingdao Innovation Leadership Program[18-1-2-12-zhc] ; Laboratory for Marine Biology and Biotechnology, Qingdao Pilot National Laboratory for Marine Science and Technology[OF2015NO12]
WOS研究方向	Biochemistry & Molecular Biology ; Chemistry ; Polymer Science
WOS类目	Biochemistry & Molecular Biology ; Chemistry, Applied ; Polymer Science
WOS记录号	WOS:000684600700007
出版者	ELSEVIER
引用统计	被引频次：2[WOS] [WOS记录] [WOS相关记录]
文献类型	期刊论文
条目标识符	http://ir.qdio.ac.cn/handle/337002/176008
专题	实验海洋生物学重点实验室
通讯作者	Ma, Qingjun
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Nanhai Rd 7, Qingdao 266071, Peoples R China 2.Pilot Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao, Peoples R China 3.Univ Chinese Acad Sci, Beijing, Peoples R China 4.Chinese Acad Sci, Ctr Ocean Megasci, Qingdao, Peoples R China 5.Ocean Univ China, Coll Marine Life Sci, Qingdao, Peoples R China
第一作者单位	中国科学院海洋研究所
通讯作者单位	中国科学院海洋研究所; 中国科学院海洋大科学研究中心
推荐引用方式 GB/T 7714	Wang, Fang,Liu, Changshui,Wang, Chongyang,et al. Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase[J]. INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,2021,184:821-830.
APA	Wang, Fang.,Liu, Changshui.,Wang, Chongyang.,Wang, Yan.,Zang, Kun.,...&Ma, Qingjun.(2021).Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase.INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES,184,821-830.
MLA	Wang, Fang,et al."Structural basis of staphylococcal Stl inhibition on a eukaryotic dUTPase".INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES 184(2021):821-830.

条目包含的文件
文件名称/大小	文献类型	版本类型	开放类型	使用许可
1-s2.0-S014181302101（2684KB）	期刊论文	出版稿	限制开放	CC BY-NC-SA	浏览