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TitleAssembly mechanism of a Tad secretion system secretin-pilotin complex.
Journal, issue, pagesNat Commun, Vol. 14, Issue 1, Page 5643, Year 2023
Publish dateSep 13, 2023
AuthorsMatteo Tassinari / Marta Rudzite / Alain Filloux / Harry H Low /
PubMed AbstractThe bacterial Tight adherence Secretion System (TadSS) assembles surface pili that drive cell adherence, biofilm formation and bacterial predation. The structure and mechanism of the TadSS is mostly ...The bacterial Tight adherence Secretion System (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.
External linksNat Commun / PubMed:37704603 / PubMed Central
MethodsEM (single particle)
Resolution2.7 - 3.6 Å
Structure data

16810

8odn

EMDB-16810, PDB-8odn:
RcpA-TadD with C13 symmetry from the Pseudomonas aeruginosa Tight Adherence Secretion System
Method: EM (single particle) / Resolution: 2.7 Å

EMDB-16818: RcpA-TadD local refinement map
Method: EM (single particle) / Resolution: 3.6 Å

Source
  • pseudomonas aeruginosa pao1 (bacteria)
KeywordsMEMBRANE PROTEIN / Secretin / Pilotin / RcpA / TadD / TAD

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