7ACV

SLPL/HID (LMW SLP complex with HMW SLP interacting domain - HID) from C. difficile (R7404 strain)

7ACV の概要

• エントリーDOI: 10.2210/pdb7acv/pdb
• 関連するPDBエントリー: 7ACW 7ACX 7ACY 7ACZ
• 分子名称: LMW SLP, HID - interacting domain of SLP HMW (3 entities in total)
• 機能のキーワード: bacterial surface layer protein, slp lmw, slp hmw interacting domain (hid), structural protein
• 由来する生物種: Clostridioides difficile; 詳細
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 73810.24

構造登録者

Barwinska-Sendra, A.,Lanzoni-Mangutchi, P.,Salgado, P.S. (登録日: 2020-09-11, 公開日: 2022-03-09, 最終更新日: 2024-01-31)

主引用文献

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

実験手法

X-RAY DIFFRACTION (2.4 Å)