7QGQ

Extended H/L (SLPH/SLPL) complex from C. difficile (CD630 strain) fit into R20291 S-layer negative stain map

This is a non-PDB format compatible entry.

Summary for 7QGQ

• Entry DOI: 10.2210/pdb7qgq/pdb
• EMDB information: 13957
• Descriptor: Precursor of the S-layer proteins (2 entities in total)
• Functional Keywords: bacterial surface, s-layer, structural protein
• Biological source: Clostridioides difficile 630; More
• Total number of polymer chains: 24
• Total formula weight: 881337.84

Authors

Banerji, O.,Wilson, J.S.,Bullough, P.A. (deposition date: 2021-12-09, release date: 2022-04-06, Last modification date: 2024-07-17)

Primary citation

Lanzoni-Mangutchi, P.,Banerji, O.,Wilson, J.,Barwinska-Sendra, A.,Kirk, J.A.,Vaz, F.,O'Beirne, S.,Basle, A.,El Omari, K.,Wagner, A.,Fairweather, N.F.,Douce, G.R.,Bullough, P.A.,Fagan, R.P.,Salgado, P.S.
Structure and assembly of the S-layer in C. difficile.
Nat Commun, 13:970-970, 2022

PubMed Abstract: Many bacteria and archaea possess a two-dimensional protein array, or S-layer, that covers the cell surface and plays crucial roles in cell physiology. Here, we report the crystal structure of SlpA, the main S-layer protein of the bacterial pathogen Clostridioides difficile, and use electron microscopy to study S-layer organisation and assembly. The SlpA crystal lattice mimics S-layer assembly in the cell, through tiling of triangular prisms above the cell wall, interlocked by distinct ridges facing the environment. Strikingly, the array is very compact, with pores of only ~10 Å in diameter, compared to other S-layers (30-100 Å). The surface-exposed flexible ridges are partially dispensable for overall structure and assembly, although a mutant lacking this region becomes susceptible to lysozyme, an important molecule in host defence. Thus, our work gives insights into S-layer organisation and provides a basis for development of C. difficile-specific therapeutics.

PubMed: 35217634
DOI: 10.1038/s41467-022-28196-w

Experimental method

ELECTRON CRYSTALLOGRAPHY