8PFB

Structure of a heteropolymeric type 4 pilus from a monoderm bacterium

Summary for 8PFB

• Entry DOI: 10.2210/pdb8pfb/pdb
• EMDB information: 17645
• Descriptor: Type IV pilin PilE1 (1 entity in total)
• Functional Keywords: bacterial pilus type 4 pilus, protein fibril
• Biological source: Streptococcus sanguinis
• Total number of polymer chains: 9
• Total formula weight: 132771.80

Authors

Anger, R.,Pieulle, L.,Shahin, M.,Valette, O.,Le Guenno, H.,Kosta, A.,Pelicic, V.,Fronzes, R. (deposition date: 2023-06-15, release date: 2023-11-22, Last modification date: 2025-07-09)

Primary citation

Anger, R.,Pieulle, L.,Shahin, M.,Valette, O.,Le Guenno, H.,Kosta, A.,Pelicic, V.,Fronzes, R.
Structure of a heteropolymeric type 4 pilus from a monoderm bacterium.
Nat Commun, 14:7143-7143, 2023

PubMed Abstract: Type 4 pili (T4P) are important virulence factors, which belong to a superfamily of nanomachines ubiquitous in prokaryotes, called type 4 filaments (T4F). T4F are defined as helical polymers of type 4 pilins. Recent advances in cryo-electron microscopy (cryo-EM) led to structures of several T4F, revealing that the long N-terminal α-helix (α1) - the trademark of pilins - packs in the centre of the filaments to form a hydrophobic core. In diderm bacteria - all available bacterial T4F structures are from diderm species - a portion of α1 is melted (unfolded). Here we report that this architecture is conserved in phylogenetically distant monoderm species by determining the structure of Streptococcus sanguinis T4P. Our 3.7 Å resolution cryo-EM structure of S. sanguinis heteropolymeric T4P and the resulting full atomic model including all minor pilins highlight universal features of bacterial T4F and have widespread implications in understanding T4F biology.

PubMed: 37932265
DOI: 10.1038/s41467-023-42872-5

Experimental method

ELECTRON MICROSCOPY (3.67 Å)