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Structural basis for specific calcium binding by the polycystic-kidney-disease domain of Vibrio anguillarum protease Epp
Li, Peihai1,2,3; Zang, Kun1,2,3; Li, Yingjie1,2; Liu, Changshui1,2; Ma, Qingjun1,2,4
2018-10-28
Source PublicationBIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
ISSN0006-291X
Volume505Issue:2Pages:471-477
Corresponding AuthorMa, Qingjun(qma@qdio.ac.cn)
AbstractExtracellular 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.
KeywordVibrio anguillarum Polycystic-kidney-disease domain Protease maturation Ca2+-binding site Protein stability
DOI10.1016/j.bbrc.2018.09.108
Indexed BySCI
Language英语
Funding Project1000-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 Research AreaBiochemistry & Molecular Biology ; Biophysics
WOS SubjectBiochemistry & Molecular Biology ; Biophysics
WOS IDWOS:000448628600022
PublisherACADEMIC PRESS INC ELSEVIER SCIENCE
Citation statistics
Document Type期刊论文
Identifierhttp://ir.qdio.ac.cn/handle/337002/156559
Collection实验海洋生物学重点实验室
Corresponding AuthorMa, Qingjun
Affiliation1.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
First Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Corresponding Author AffilicationInstitute of Oceanology, Chinese Academy of Sciences
Recommended Citation
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.
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