ArticleNature communications2018
Molecular basis for the folding of β-helical autotransporter passenger domains.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed.
- SeaB is a conservedInfection and immunity · 2026Article
- Mutations affecting the β-sheet at the extracellular opening of the intimin β-barrel domain lead to reduced protein levels and inefficient passenger secretion.Bioscience reports · 2026Article
- EnteroaggregativeEcoSal Plus · 2025Review
- Host cyclophilin-mediated maturation of an obligate intracellular bacterial surface virulence factor.bioRxiv : the preprint server for biology · 2025Article
- Autoproteolytic mechanism of CdiA toxin release reconstitutedJournal of bacteriology · 2024Article
- Sequence, structure prediction, and epitope analysis of the polymorphic membrane protein family in Chlamydia trachomatis.PloS one · 2024Article
- Phospholipids are imported into mitochondria by VDAC, a dimeric beta barrel scramblase.Nature communications · 2023Article
- Uncovering the folding mechanism of pertactin: A comparative study of isolated and vectorial folding.Biophysical journal · 2023Article
- Article
- Detergent headgroups control TolC folding in vitro.Biophysical journal · 2023Article
- Protein import and export across the bacterial outer membrane.Current opinion in structural biology · 2021Review
- Folding Control in the Path of Type 5 Secretion.Toxins · 2021Review
- BamA forms a translocation channel for polypeptide export across the bacterial outer membrane.Molecular cell · 2021Article
- The rhizobial autotransporter determines the symbiotic nitrogen fixation activity ofProceedings of the National Academy of Sciences of the United States of America · 2020Article
- Chaperone OsmY facilitates the biogenesis of a major family of autotransporters.Molecular microbiology · 2019Article
- Type V Secretion in Gram-Negative Bacteria.EcoSal Plus · 2019Article
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Authors and funding
10 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Bacterial autotransporters comprise a C-terminal β-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 β-helix. In a cellular context, key molecules catalyze the assembly of the autotransporter β-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 β-hairpin structure of the fifth extracellular loop of the β-barrel domain has a crucial role for passenger domain folding into a β-helix. Bioinformatics and structural analyses, and mutagenesis of a homologous autotransporter, suggest that this function is conserved among autotransporter proteins with β-helical passenger domains. We propose that the autotransporter β-barrel domain is a folding vector that nucleates folding of the passenger domain.
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