Journal: Nat Commun / Year: 2023 Title: Structure of a heteropolymeric type 4 pilus from a monoderm bacterium. Authors: Robin Anger / Laetitia Pieulle / Meriam Shahin / Odile Valette / Hugo Le Guenno / Artemis Kosta / Vladimir Pelicic / Rémi Fronzes / 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 ...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.
G: Type IV pilin PilE1 F: Type IV pilin PilE1 C: Type IV pilin PilE1 A: Type IV pilin PilE1 B: Type IV pilin PilE1 I: Type IV pilin PilE1 H: Type IV pilin PilE1 D: Type IV pilin PilE1 E: Type IV pilin PilE1
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