Secretion mechanism of the autotransporter proteins. (A) Structure of
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Last updated 29 mai 2024
Download scientific diagram | Secretion mechanism of the autotransporter proteins. (A) Structure of the polyprotein precursor. (B) Transport of the recombinant passenger. By the use of a typical signal peptide, a precursor protein is transported across the inner membrane. After arrival at the periplasm, the C-terminal part of the precursor folds as a porin-like structure, a so-called  -barrel within the outer membrane, and the passenger is transmitted to the cell surface. SP, signal peptide; IM, inner membrane; PP, periplasm; OM, outer membrane. from publication: The Autodisplay Story, from Discovery to Biotechnical and Biomedical Applications | Among the pathways used by gram-negative bacteria for protein secretion, the autotransporter pathway represents a solution of impressive simplicity. Proteins are transported, independent of their nature as recombinant or native passengers, as long as the coding nucleotide | Biomedical Applications, Escherichia Coli Adhesins and Neisseria gonorrhoeae | ResearchGate, the professional network for scientists.
Secretion systems in Gram-negative bacteria: structural and mechanistic insights
A structurally informed autotransporter platform for efficient heterologous protein secretion and display, Microbial Cell Factories
Mechanistic link between β barrel assembly and the initiation of autotransporter secretion
Autotransporter proteins, evolution and redefining protein secretion: Trends in Microbiology
Autotransporter secretion: varying on a theme - ScienceDirect
Crystal structure of a subtilisin-like autotransporter passenger domain reveals insights into its cytotoxic function
Type V secretion: From biogenesis to biotechnology - ScienceDirect
Structure, secretion mechanism, cytoplasm translocation
Virulence Functions of Autotransporter Proteins
KEGG PATHWAY: ko03070
Autotransporter protein structure and secretion. Autotransporter
Type V secretion: mechanism(s) of autotransport through the bacterial outer membrane
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