Metadata
Show full item recordShare this item!
Structure of a heteropolymeric type 4 pilus from a monoderm bacterium
SHAHIN, Meriam
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
See more >
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
SHAHIN, Meriam
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
MRC Centre for Molecular Microbiology and Infection [Imperial College, London] [CMBI]
VALETTE, Odile
Laboratoire de chimie bactérienne [LCB]
Institut de Microbiologie de la Méditerranée [IMM]
Laboratoire de chimie bactérienne [LCB]
Institut de Microbiologie de la Méditerranée [IMM]
PELICIC, Vladimir
Institut National de la Santé et de la Recherche Médicale [INSERM]
Laboratoire de chimie bactérienne [LCB]
Institut National de la Santé et de la Recherche Médicale [INSERM]
Laboratoire de chimie bactérienne [LCB]
FRONZES, Remi
Institut Européen de Chimie et Biologie [IECB]
Microbiologie Fondamentale et Pathogénicité [MFP]
< Reduce
Institut Européen de Chimie et Biologie [IECB]
Microbiologie Fondamentale et Pathogénicité [MFP]
Language
EN
Article de revue
This item was published in
Nature Communications. 2023-12, vol. 14, n° 1, p. 7143
English Abstract
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. ...Read more >
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.Read less <
ANR Project
Analyse structure/fonction du pilus Com, nanomachine filamenteuse répandue chez les bactéries monodermes, dédiée à la capture d'ADN - ANR-21-CE11-0008