8ODN

RcpA-TadD with C13 symmetry from the Pseudomonas aeruginosa Tight Adherence Secretion System

This is a non-PDB format compatible entry.

Summary for 8ODN

• Entry DOI: 10.2210/pdb8odn/pdb
• EMDB information: 16810
• Descriptor: RcpA, TPR repeat-containing protein PA4299 (2 entities in total)
• Functional Keywords: secretin, pilotin, rcpa, tadd, tad, membrane protein
• Biological source: Pseudomonas aeruginosa PAO1; More
• Total number of polymer chains: 26
• Total formula weight: 952471.65

Authors

Tassinari, M.,Low, H.H. (deposition date: 2023-03-09, release date: 2023-09-27, Last modification date: 2024-11-13)

Primary citation

Tassinari, M.,Rudzite, M.,Filloux, A.,Low, H.H.
Assembly mechanism of a Tad secretion system secretin-pilotin complex.
Nat Commun, 14:5643-5643, 2023

PubMed Abstract: 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.

PubMed: 37704603
DOI: 10.1038/s41467-023-41200-1

Experimental method

ELECTRON MICROSCOPY (2.7 Å)