7ACV
SLPL/HID (LMW SLP complex with HMW SLP interacting domain - HID) from C. difficile (R7404 strain)
Summary for 7ACV
| Entry DOI | 10.2210/pdb7acv/pdb |
| Related | 7ACW 7ACX 7ACY 7ACZ |
| Descriptor | LMW SLP, HID - interacting domain of SLP HMW (3 entities in total) |
| Functional Keywords | bacterial surface layer protein, slp lmw, slp hmw interacting domain (hid), structural protein |
| Biological source | Clostridioides difficile More |
| Total number of polymer chains | 3 |
| Total formula weight | 73810.24 |
| Authors | Barwinska-Sendra, A.,Lanzoni-Mangutchi, P.,Salgado, P.S. (deposition date: 2020-09-11, release date: 2022-03-09, Last modification date: 2024-01-31) |
| 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 Cited by 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: 35217634DOI: 10.1038/s41467-022-28196-w PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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