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Conformational folding and disulfide bonding drive distinct stages of protein structure formation
Lv JM; Lv SQ(吕守芹); Liu ZP; Zhang J; Gao BoX; Yao ZY; Wu YX; Potempa LA.; Ji SR; Long M(龙勉); Wu Y(武毅)
Source PublicationSCIENTIFIC REPORTS
2018-01-24
Volume8Pages:1494
ISSN2045-2322
Abstract

The causal relationship between conformational folding and disulfide bonding in protein oxidative folding remains incompletely defined. Here we show a stage-dependent interplay between the two events in oxidative folding of C-reactive protein (CRP) in live cells. CRP is composed of five identical subunits, which first fold spontaneously to a near-native core with a correctly positioned C-terminal helix. This process drives the formation of the intra-subunit disulfide bond between Cys36 and Cys97. The second stage of subunit folding, however, is a non-spontaneous process with extensive restructuring driven instead by the intra-subunit disulfide bond and guided by calcium binding-mediated anchoring. With the folded subunits, pentamer assembly ensues. Our results argue that folding spontaneity is the major determinant that dictates which event acts as the driver. The stepwise folding pathway of CRP further suggests that one major route might be selected out of the many in theory for efficient folding in the cellular environment.

DOI10.1038/s41598-018-20014-y
Indexed BySCI ; EI
Language英语
WOS IDWOS:000423154000024
WOS KeywordC-reactive-protein ; Molecular-dynamics ; Expression ; Calcium ; Binding ; Form ; Crp
WOS Research AreaScience & Technology - Other Topics
WOS SubjectMultidisciplinary Sciences
Funding OrganizationNSFC(31470718 ; Fundamental Research Funds for the Central Universities(lzujbky-2016-k11 ; 31570749 ; lzujbky-2016-222) ; 31230027 ; 91642203)
Classification二类/q1
Ranking1
Citation statistics
Cited Times:4[WOS]   [WOS Record]     [Related Records in WOS]
Document Type期刊论文
Identifierhttp://dspace.imech.ac.cn/handle/311007/77463
Collection国家微重力实验室
Recommended Citation
GB/T 7714
Lv JM,Lv SQ,Liu ZP,et al. Conformational folding and disulfide bonding drive distinct stages of protein structure formation[J]. SCIENTIFIC REPORTS,2018,8:1494.
APA Lv JM.,吕守芹.,Liu ZP.,Zhang J.,Gao BoX.,...&武毅.(2018).Conformational folding and disulfide bonding drive distinct stages of protein structure formation.SCIENTIFIC REPORTS,8,1494.
MLA Lv JM,et al."Conformational folding and disulfide bonding drive distinct stages of protein structure formation".SCIENTIFIC REPORTS 8(2018):1494.
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