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DOI10.1038/s41467-018-04071-5
Molecular basis for the folding of beta-helical autotransporter passenger domains
Yuan, Xiaojun1; Johnson, Matthew D.1; Zhang, Jing1; Lo, Alvin W.2,3; Schembri, Mark A.2,3; Wijeyewickrema, Lakshmi C.4; Pike, Robert N.4; Huysmans, Gerard H. M.5; Henderson, Ian R.6; Leyton, Denisse L.1,7
2018-04-11
发表期刊NATURE COMMUNICATIONS
ISSN2041-1723
出版年2018
卷号9
文章类型Article
语种英语
国家Australia; USA; England
英文摘要

Bacterial autotransporters comprise a C-terminal beta-barrel domain, which must be correctly folded and inserted into the outer membrane to facilitate translocation of the N-terminal passenger domain to the cell exterior. Once at the surface, the passenger domains of most autotransporters are folded into an elongated beta-helix. In a cellular context, key molecules catalyze the assembly of the autotransporter beta-barrel domain. However, how the passenger domain folds into its functional form is poorly understood. Here we use mutational analysis on the autotransporter Pet to show that the beta-hairpin structure of the fifth extracellular loop of the beta-barrel domain has a crucial role for passenger domain folding into a beta-helix. Bioinformatics and structural analyses, and mutagenesis of a homologous autotransporter, suggest that this function is conserved among autotransporter proteins with beta-helical passenger domains. We propose that the autotransporter beta-barrel domain is a folding vector that nucleates folding of the passenger domain.


领域资源环境
收录类别SCI-E
WOS记录号WOS:000429689800018
WOS关键词ENTEROAGGREGATIVE ESCHERICHIA-COLI ; SERINE-PROTEASE AUTOTRANSPORTERS ; BACTERIAL OUTER MEMBRANES ; CRYSTAL-STRUCTURE ; VIRULENCE PROTEIN ; STRUCTURE REVEALS ; STRUCTURAL BASIS ; SECRETION ; TRANSPORT ; MECHANISM
WOS类目Multidisciplinary Sciences
WOS研究方向Science & Technology - Other Topics
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文献类型期刊论文
条目标识符http://119.78.100.173/C666/handle/2XK7JSWQ/203787
专题资源环境科学
作者单位1.Australian Natl Univ, Res Sch Biol, Canberra, ACT 0200, Australia;
2.Univ Queensland, Sch Chem & Mol Biosci, Brisbane, Qld 4072, Australia;
3.Univ Queensland, Australian Infect Dis Res Ctr, Brisbane, Qld 4072, Australia;
4.La Trobe Univ, La Trobe Inst Mol Sci, Dept Biochem & Genet, Melbourne, Vic 3086, Australia;
5.Weill Cornell Med, Dept Physiol & Biophys, New York, NY 10065 USA;
6.Univ Birmingham, Inst Microbiol & Infect, Birmingham B15 2TT, W Midlands, England;
7.Australian Natl Univ, Med Sch, Canberra, ACT 0200, Australia
推荐引用方式
GB/T 7714
Yuan, Xiaojun,Johnson, Matthew D.,Zhang, Jing,et al. Molecular basis for the folding of beta-helical autotransporter passenger domains[J]. NATURE COMMUNICATIONS,2018,9.
APA Yuan, Xiaojun.,Johnson, Matthew D..,Zhang, Jing.,Lo, Alvin W..,Schembri, Mark A..,...&Leyton, Denisse L..(2018).Molecular basis for the folding of beta-helical autotransporter passenger domains.NATURE COMMUNICATIONS,9.
MLA Yuan, Xiaojun,et al."Molecular basis for the folding of beta-helical autotransporter passenger domains".NATURE COMMUNICATIONS 9(2018).
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