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Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (pdilt) provide insight into its chaperone activity

文献类型：期刊论文

作者Li, Huanhuan1,4; Yang, Kai2,4; Wang, Wenjia3; Niu, Yingbo2,4; Li, Jun1,4; Dong, Yuhui3; Liu, Yingfang1,5; Wang, Chih-chen2,4; Wang, Lei2,4; Liang, Huanhuan1,6
刊名Journal of biological chemistry
出版日期2018-01-26
卷号293期号:4页码:1192-1202
关键词Conformational change Molecular chaperone Protein structure Small-angle x-ray scattering (saxs) X-ray crystallography
ISSN号0021-9258
DOI10.1074/jbc.m117.797290
通讯作者Wang, lei(wanglei@moon.ibp.ac.cn) ; Liang, huanhuan(hhliang@moon.ibp.ac.cn)
英文摘要Protein-disulfide isomerase-like protein of the testis (pdilt), a member of the protein-disulfide isomerase family, is a chaperone essential for the folding of spermatogenesis-specific proteins in male postmeiotic germ cells. however, the structural mechanisms that regulate the chaperone function of pdilts are unknown. here, we report the structures of human pdilt (hpdilt) determined by x-ray crystallography to 2.4 resolution and small-angle x-ray scattering (saxs). distinct from previously reported u-like structures of related pdi family proteins, our structures revealed that hpdilt folds into a compact l-like structure in crystals and into an extended chain-like structure in solution. the hydrophobic regions and the hydrophobic pockets in hpdilt, which are important for substrate recognition, were clearly delineated in the crystal structure. moreover, our results of the saxs analysis and of structure-based substitutions and truncations indicated that the c-terminal tail in hpdilt is required for suppression of aggregation of denatured proteins, suggesting that the tail is crucial for the chaperone activity of pdilt. taken together, our findings have identified the critical regions and conformational changes of pdilt that enable and control its activity. these results advance our understanding of the structural mechanisms involved in the chaperone activity of pdilt.
WOS关键词SMALL-ANGLE SCATTERING ; REDOX-REGULATED CHAPERONE ; RAY SOLUTION SCATTERING ; MHC CLASS-I ; ENDOPLASMIC-RETICULUM ; BIOLOGICAL MACROMOLECULES ; MISFOLDED PROTEINS ; FOLDING CATALYST ; QUALITY-CONTROL ; BINDING SITE
WOS研究方向Biochemistry & Molecular Biology
WOS类目Biochemistry & Molecular Biology
语种英语
WOS记录号WOS:000423515000008
出版者AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
URI标识http://www.irgrid.ac.cn/handle/1471x/2177944
专题高能物理研究所
通讯作者Wang, Lei; Liang, Huanhuan
作者单位1.Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromol, Natl Lab Biomacromol, Beijing 100101, Peoples R China
2.Chinese Acad Sci, Inst Biophys, CAS Ctr Excellence Biomacromol, Natl Lab Biomacromol, Beijing 100101, Peoples R China
3.Chinese Acad Sci, Inst High Energy Phys, Beijing Synchrotron Radiat Facil, Beijing 100049, Peoples R China
4.Univ Chinese Acad Sci, Coll Life Sci, Beijing 100049, Peoples R China
5.Sun Yat Sen Univ, Sch Med, Guangzhou 510275, Guangdong, Peoples R China
6.Sun Yat Sen Univ, Sch Pharmaceut Sci Shenzhen, Guangzhou 510275, Guangdong, Peoples R China
推荐引用方式
GB/T 7714		 Li, Huanhuan,Yang, Kai,Wang, Wenjia,et al. Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (pdilt) provide insight into its chaperone activity[J]. Journal of biological chemistry,2018,293(4):1192-1202.
APA Li, Huanhuan.,Yang, Kai.,Wang, Wenjia.,Niu, Yingbo.,Li, Jun.,...&Liang, Huanhuan.(2018).Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (pdilt) provide insight into its chaperone activity.Journal of biological chemistry,293(4),1192-1202.
MLA Li, Huanhuan,et al."Crystal and solution structures of human protein-disulfide isomerase-like protein of the testis (pdilt) provide insight into its chaperone activity".Journal of biological chemistry 293.4(2018):1192-1202.

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