IR@PKUHSC  > 北京大学基础医学院  > 北京大学系统生物医学研究所
学科主题基础医学
Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function
Liu, Liang1,2,3; Chen, Ji-Yun1,2; Yang, Bo3; Wang, Fang-Hua4; Wang, Yong-Hua4; Yun, Cai-Hong1,2
刊名STRUCTURE
2015-11-03
DOI10.1016/j.str.2015.08.015
23期:11页:2066-2075
收录类别SCI
文章类型Article
WOS标题词Science & Technology
类目[WOS]Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
资助者National Basic Research Program of China (973 Program) ; National Science Foundation of China ; Ministry of Science and Technology of China ; National Science Funds for the Excellent Youth Scholars ; fundamental Research Funds for the Central Universities ; National Basic Research Program of China (973 Program) ; National Science Foundation of China ; Ministry of Science and Technology of China ; National Science Funds for the Excellent Youth Scholars ; fundamental Research Funds for the Central Universities
研究领域[WOS]Biochemistry & Molecular Biology ; Biophysics ; Cell Biology
关键词[WOS]ALPHA-B-CRYSTALLIN ; SUBSTRATE-BINDING ; UNFOLDED PROTEIN ; T4 LYSOZYME ; DOMAIN ; SOFTWARE ; HSP16.5 ; STRESS ; HSP26 ; OLIGOMERIZATION
英文摘要

Small heat-shock proteins (sHsps) maintain cellular homeostasis by binding to denatured client proteins to prevent aggregation. Numerous studies indicate that the N-terminal domain (NTD) of sHsps is responsible for binding to client proteins, but the binding mechanism and chaperone activity regulation remain elusive. Here, we report the crystal structures of the wild-type and mutants of an sHsp from Sulfolobus solfataricus representing the inactive and active state of this protein, respectively. All three structures reveal well-defined NTD, but their conformations are remarkably different. The mutant NTDs show disrupted helices presenting a reformed hydrophobic surface compatible with recognizing client proteins. Our functional data show that mutating key hydrophobic residues in this region drastically altered the chaperone activity of this sHsp. These data suggest a new model in which a molecular switch located in NTD facilitates conformational changes for client protein binding.

语种英语
所属项目编号2012CB917202 ; 31270769 ; NCET-12-0013 ; 31222043 ; 2014ZM0062
资助者National Basic Research Program of China (973 Program) ; National Science Foundation of China ; Ministry of Science and Technology of China ; National Science Funds for the Excellent Youth Scholars ; fundamental Research Funds for the Central Universities ; National Basic Research Program of China (973 Program) ; National Science Foundation of China ; Ministry of Science and Technology of China ; National Science Funds for the Excellent Youth Scholars ; fundamental Research Funds for the Central Universities
WOS记录号WOS:000366170300013
Citation statistics
Cited Times:2[WOS]   [WOS Record]     [Related Records in WOS]
文献类型期刊论文
条目标识符http://ir.bjmu.edu.cn/handle/400002259/54662
Collection北京大学基础医学院_北京大学系统生物医学研究所
作者单位1.Peking Univ, Beijing Key Lab Tumor Syst Biol, Hlth Sci Ctr, Inst Syst Biomed,Dept Biophys,Sch Basic Med Sci, Beijing 100191, Peoples R China
2.Peking Univ, Hlth Sci Ctr, Sch Basic Med Sci, Ctr Mol & Translat Med, Beijing 100191, Peoples R China
3.S China Univ Technol, Sch Biosci & Bioengn, Guangzhou 510006, Guangdong, Peoples R China
4.S China Univ Technol, Coll Light Ind & Food Sci, Guangzhou 510641, Guangdong, Peoples R China
Recommended Citation
GB/T 7714
Liu, Liang,Chen, Ji-Yun,Yang, Bo,et al. Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function[J]. STRUCTURE,2015,23(11):2066-2075.
APA Liu, Liang,Chen, Ji-Yun,Yang, Bo,Wang, Fang-Hua,Wang, Yong-Hua,&Yun, Cai-Hong.(2015).Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function.STRUCTURE,23(11),2066-2075.
MLA Liu, Liang,et al."Active-State Structures of a Small Heat-Shock Protein Revealed a Molecular Switch for Chaperone Function".STRUCTURE 23.11(2015):2066-2075.
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