Institutional Repository of Key Laboratory of Experimental Marine Biology, Institute of Oceanology, Chinese Academy of Sciences
The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner | |
Zang, Kun1,2,3; Li, Fuhua1,2; Ma, Qingjun1,2 | |
2018-01-19 | |
发表期刊 | JOURNAL OF BIOLOGICAL CHEMISTRY |
卷号 | 293期号:3页码:1088-1099 |
文章类型 | Article |
摘要 | dUTPases are essential enzymes for maintaining genome integrity and have recently been shown to play moonlighting roles when containing extra sequences. Interestingly, the trimeric dUTPase of white spot syndrome virus (wDUT) harbors a sequence insert at the position preceding the C-terminal catalytic motifV(pre-V insert), rarely seen in other dUTPases. However, whether this extra sequence endowswDUTwith additional properties is unknown. Herein, we present the crystal structures of wDUT in both ligand-free and ligand-bound forms. We observed that the pre-V insert in wDUT forms an unusual beta-hairpin structure in the domain-swapping region and thereby facilitates a unique orientation of the adjacent C-terminal segment, positioning the catalytic motif V onto the active site of its own subunit instead of a third subunit. Consequently, wDUT employs two-subunit active sites, unlike the widely accepted paradigm that the active site of trimeric dUTPase is contributed by all three subunits. According to results from local structural comparisons, the active-site configuration ofwDUTis similar to that of known dUTPases. However, we also found that residues in the second-shell region of the active site are reconfigured in wDUT as an adaption to its unique C-terminal orientation. We also show that deletion of the pre-V insert significantly reduces wDUT's enzymatic activity and thermal stability. We hypothesize that this rare structural arrangement confers additional functionality to wDUT. In conclusion, our study expands the structural diversity in the conserved dUTPase family and illustrates how sequence insertion and amino acid substitution drive protein evolution cooperatively. |
DOI | 10.1074/jbc.M117.815266 |
收录类别 | SCI |
语种 | 英语 |
WOS记录号 | WOS:000422864500027 |
引用统计 | |
文献类型 | 期刊论文 |
版本 | 出版稿 |
条目标识符 | http://ir.qdio.ac.cn/handle/337002/154331 |
专题 | 实验海洋生物学重点实验室 |
作者单位 | 1.Chinese Acad Sci, Inst Oceanol, Key Lab Expt Marine Biol, Nanhai Rd 7, Qingdao 266071, Peoples R China 2.Qingdao Natl Lab Marine Sci & Technol, Lab Marine Biol & Biotechnol, Qingdao 266237, Peoples R China 3.Univ Chinese Acad Sci, Beijing 100049, Peoples R China |
第一作者单位 | 中国科学院海洋研究所 |
推荐引用方式 GB/T 7714 | Zang, Kun,Li, Fuhua,Ma, Qingjun. The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2018,293(3):1088-1099. |
APA | Zang, Kun,Li, Fuhua,&Ma, Qingjun.(2018).The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner.JOURNAL OF BIOLOGICAL CHEMISTRY,293(3),1088-1099. |
MLA | Zang, Kun,et al."The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner".JOURNAL OF BIOLOGICAL CHEMISTRY 293.3(2018):1088-1099. |
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 | ||
The dUTPase of white(2718KB) | 期刊论文 | 出版稿 | 限制开放 | CC BY-NC-SA | 浏览 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论