Wzb of Vibrio vulnificus represents a new group of low-molecular-weight protein tyrosine phosphatases with a unique insertion in the W-loop

doi:10.1016/j.jbc.2021.100280

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	Wzb of Vibrio vulnificus represents a new group of low-molecular-weight protein tyrosine phosphatases with a unique insertion in the W-loop
	Wang, Xin 1,2,3; Ma, Qingjun 1,2,3,4
刊名	JOURNAL OF BIOLOGICAL CHEMISTRY
	2021
卷号	296 页码:13
DOI	10.1016/j.jbc.2021.100280
通讯作者	Ma, Qingjun(qma@qdio.ac.cn)
英文摘要	Protein tyrosine phosphorylation regulates the production of capsular polysaccharide, an essential virulence factor of the deadly pathogen Vibrio vulnificus. The process requires the protein tyrosine kinase Wzc and its cognate phosphatase Wzb, both of which are largely uncharacterized. Herein, we report the structures of Wzb of V. vulnificus (VvWzb) in free and ligand-bound forms. VvWzb belongs to the low-molecular-weight protein tyrosine phosphatase (LMWPTP) family. Interestingly, it contains an extra four-residue insertion in the W-loop, distinct from all known LMWPTPs. The W-loop of VvWzb protrudes from the protein body in the free structure, but undergoes significant conformational changes to fold toward the active site upon ligand binding. Deleting the four-residue insertion from the W-loop severely impaired the enzymatic activity of VvWzb, indicating its importance for optimal catalysis. However, mutating individual residues or even substituting the whole insertion with four alanine residues only modestly decreased the enzymatic activity, suggesting that the contribution of the insertion to catalysis is not determined by the sequence specificity. Furthermore, inserting the four residues into Escherichia coli Wzb at the corresponding position enhanced its activity as well, indicating that the four-residue insertion in the W-loop can act as a general activity enhancing element for other LMWPTPs. The novel W-loop type and phylogenetic analysis suggested that VvWzb and its homologs should be classified into a new group of LMWPTPs. Our study sheds new insight into the catalytic mechanism and structural diversity of the LMWPTP family and promotes the understanding of the protein tyrosine phosphorylation system in prokaryotes.
资助项目	Qingdao Innovation Leadership Program[18-1-2-12-zhc] ; Aoshan Talents Program of the Pilot National Laboratory for Marine Science and Technology[2015ASTP]
WOS研究方向	Biochemistry & Molecular Biology
语种	英语
出版者	ELSEVIER
WOS记录号	WOS:000672866400256
内容类型	期刊论文
源URL	[http://ir.qdio.ac.cn/handle/337002/176224]
专题	海洋研究所_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.Pilot 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	Wang, Xin,Ma, Qingjun. Wzb of Vibrio vulnificus represents a new group of low-molecular-weight protein tyrosine phosphatases with a unique insertion in the W-loop[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2021,296:13.
APA	Wang, Xin,&Ma, Qingjun.(2021).Wzb of Vibrio vulnificus represents a new group of low-molecular-weight protein tyrosine phosphatases with a unique insertion in the W-loop.JOURNAL OF BIOLOGICAL CHEMISTRY,296,13.
MLA	Wang, Xin,et al."Wzb of Vibrio vulnificus represents a new group of low-molecular-weight protein tyrosine phosphatases with a unique insertion in the W-loop".JOURNAL OF BIOLOGICAL CHEMISTRY 296(2021):13.