IOCAS-IR  > 实验海洋生物学重点实验室
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
Source PublicationJOURNAL OF BIOLOGICAL CHEMISTRY
Volume293Issue:3Pages:1088-1099
SubtypeArticle
AbstractdUTPases 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.
DOI10.1074/jbc.M117.815266
Indexed BySCI
Language英语
WOS IDWOS:000422864500027
Citation statistics
Cited Times:1[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Version出版稿
Identifierhttp://ir.qdio.ac.cn/handle/337002/154331
Collection实验海洋生物学重点实验室
Affiliation1.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
First Author Affilication中国科学院海洋研究所
Recommended Citation
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.
Files in This Item:
File Name/Size DocType Version Access License
The dUTPase of white(2718KB)期刊论文出版稿开放获取CC BY-NC-SAView Application Full Text
Related Services
Recommend this item
Bookmark
Usage statistics
Export to Endnote
Google Scholar
Similar articles in Google Scholar
[Zang, Kun]'s Articles
[Li, Fuhua]'s Articles
[Ma, Qingjun]'s Articles
Baidu academic
Similar articles in Baidu academic
[Zang, Kun]'s Articles
[Li, Fuhua]'s Articles
[Ma, Qingjun]'s Articles
Bing Scholar
Similar articles in Bing Scholar
[Zang, Kun]'s Articles
[Li, Fuhua]'s Articles
[Ma, Qingjun]'s Articles
Terms of Use
No data!
Social Bookmark/Share
File name: The dUTPase of white spot syndrome virus assembles its active sites in a noncanonical manner .pdf
Format: Adobe PDF
All comments (0)
No comment.
 

Items in the repository are protected by copyright, with all rights reserved, unless otherwise indicated.