Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
| 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 | |
| 发表期刊 | BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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| ISSN | 0006-291X |
| 卷号 | 505期号:2页码:471-477 |
| 通讯作者 | Ma, Qingjun(qma@qdio.ac.cn) |
| 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 |
| 收录类别 | SCI |
| 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] ; 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 |
| 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.qdio.ac.cn/handle/337002/156559 |
| 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, 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 |
| 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 | 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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