Matches in SemOpenAlex for { <https://semopenalex.org/work/W4386710757> ?p ?o ?g. }
- W4386710757 abstract "Abstract The bacterial T ight ad herence S ecretion S ystem (TadSS) assembles surface pili that drive cell adherence, biofilm formation and bacterial predation. The structure and mechanism of the TadSS is mostly unknown. This includes characterisation of the outer membrane secretin through which the pilus is channelled and recruitment of its pilotin. Here we investigate RcpA and TadD lipoprotein from Pseudomonas aeruginosa . Light microscopy reveals RcpA colocalising with TadD in P. aeruginosa and when heterologously expressed in Escherichia coli . We use cryogenic electron microscopy to determine how RcpA and TadD assemble a secretin channel with C13 and C14 symmetries. Despite low sequence homology, we show that TadD shares a similar fold to the type 4 pilus system pilotin PilF. We establish that the C-terminal four residues of RcpA bind TadD - an interaction essential for secretin formation. The binding mechanism between RcpA and TadD appears distinct from known secretin-pilotin pairings in other secretion systems." @default.
- W4386710757 created "2023-09-14" @default.
- W4386710757 creator A5008041421 @default.
- W4386710757 creator A5031492621 @default.
- W4386710757 creator A5078724972 @default.
- W4386710757 creator A5087158826 @default.
- W4386710757 date "2023-09-13" @default.
- W4386710757 modified "2023-09-29" @default.
- W4386710757 title "Assembly mechanism of a Tad secretion system secretin-pilotin complex" @default.
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- W4386710757 doi "https://doi.org/10.1038/s41467-023-41200-1" @default.
- W4386710757 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/37704603" @default.
- W4386710757 hasPublicationYear "2023" @default.
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