Global S&T Development Trend Analysis Platform of Resources and Environment
DOI | 10.1038/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
![]() |
ISSN | 2041-1723 |
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 |
URL | 查看原文 |
引用统计 | |
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). |
条目包含的文件 | 条目无相关文件。 |
除非特别说明,本系统中所有内容都受版权保护,并保留所有权利。
修改评论