Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein

The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukary...

Full description

Saved in:
Bibliographic Details
Published in:PloS one 2021-07, Vol.16 (7), p.e0254232-e0254232
Main Authors: Nguyen, Van Son, Spinelli, Silvia, Cascales, Éric, Roussel, Alain, Cambillau, Christian, Leone, Philippe
Format: Article
Language:English
Subjects:
Analysis
Bacteria
Binding sites
Biology and Life Sciences
Cell walls
Chromatography
Crystal structure
Crystallization
Crystals
Data collection
Domains
Gram-negative bacteria
Life Sciences
Medicine and Health Sciences
Peptidoglycans
Physical Sciences
Protein binding
Proteins
Structure
Virulence
Virulence factors
Citations: Items that this one cites
Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved.
ISSN:1932-6203
1932-6203
DOI:10.1371/journal.pone.0254232