Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp

doi:10.1016/j.bbrc.2018.09.108

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	Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp
	Li, Peihai 1,2,3; Zang, Kun 1,2,3; Li, Yingjie 1,2; Liu, Changshui 1,2; Ma, Qingjun 1,2,4
	2018-10-28
发表期刊	BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN	0006-291X
卷号	505 期号:2 页码:471-477
摘要	Extracellular proteases are often produced as pre-pro-enzyme and then undergo multiple processing steps to mature into the active form. The protease Epp, a virulent factor of Vibrio anguillarum, belongs to this family. Its maturation might be regulated by Ca2+ via its polycystic kidney disease (PKD) domain, but the molecular mechanism is unknown. Herein, we report the crystal structure of the first PKD domain from V. anguillarum Epp (Epp-PKD1) and its specific Ca2+ -binding capacity. Epp-PKD1 exists as a monomer, consisting of seven beta-strands which form two beta-sheets stacking with each other. One Ca2+ is bound by the residues Asn3, Gln4, Asp27, Asp29, Asp68 and a water molecule with a pentagonal bipyramidal geometry. Incubating the apo Epp-PKD1 with Ca2+ but not Mg2+, Mn2+, or Zn2+, enhances the thermal and chemical stability of Epp-PKD1, indicating its specific binding to Ca2+. Epp-PKD1 shares high similarity in both sequence and overall structure with that of Vibrio cholerae PrtV, a homologous protease of Epp, however, they differ in the oligomeric state and local structure at the Ca2+-binding site, suggesting maturation of PrtV and Epp might be differently regulated by Ca2+. Likely, proteases may take advantage of the structural diversity in PKD domains to tune their Ca2+-regulated maturation process. (C) 2018 Elsevier Inc. All rights reserved.
关键词	Vibrio anguillarum Polycystic-kidney-disease domain Protease maturation Ca2+-binding site Protein stability
DOI	10.1016/j.bbrc.2018.09.108
关键词[WOS]	METALLOPROTEASE PRTV ; PROTEINS ; CHOLERAE ; IDENTIFICATION ; DEGRADATION ; SOFTWARE ; FEATURES ; COLLAGEN ; TOOL
语种	英语
资助项目	1000-talents program ; "100-talents Project" of Chinese Academy of Sciences ; "AoShan Talents Program" of Qingdao National Laboratory for Marine Science and Technology[2015ASTP] ; Qingdao Innovation Leadership Project[17-12-03-0006]
WOS研究方向	Biochemistry & Molecular Biology ; Biophysics
项目资助者	1000-talents program ; "100-talents Project" of Chinese Academy of Sciences ; "AoShan Talents Program" of Qingdao National Laboratory for Marine Science and Technology ; Qingdao Innovation Leadership Project
WOS类目	Biochemistry & Molecular Biology ; Biophysics
WOS记录号	WOS:000448628600022
出版者	ACADEMIC PRESS INC ELSEVIER SCIENCE
引用统计
文献类型	期刊论文
条目标识符	http://ir.qibebt.ac.cn/handle/337004/11211
专题	中国科学院青岛生物能源与过程研究所
通讯作者	Ma, Qingjun
作者单位	1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Qingdao, Peoples R China 2.Qingdao 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
推荐引用方式 GB/T 7714	Li, Peihai,Zang, Kun,Li, Yingjie,et al. Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp[J]. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,2018,505(2):471-477.
APA	Li, Peihai,Zang, Kun,Li, Yingjie,Liu, Changshui,&Ma, Qingjun.(2018).Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp.BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS,505(2),471-477.
MLA	Li, Peihai,et al."Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp".BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 505.2(2018):471-477.