8OPR
Structure of the EA1 surface layer of Bacillus anthracis
Summary for 8OPR
| Entry DOI | 10.2210/pdb8opr/pdb |
| Descriptor | S-layer protein EA1, Nanobody 643, Nanobody 632, ... (7 entities in total) |
| Functional Keywords | s-layer, ea1, anthrax, structural protein |
| Biological source | Bacillus anthracis More |
| Total number of polymer chains | 3 |
| Total formula weight | 100459.95 |
| Authors | Sogues, A.,Remaut, H. (deposition date: 2023-04-07, release date: 2023-11-08, Last modification date: 2024-11-06) |
| Primary citation | Sogues, A.,Fioravanti, A.,Jonckheere, W.,Pardon, E.,Steyaert, J.,Remaut, H. Structure and function of the EA1 surface layer of Bacillus anthracis. Nat Commun, 14:7051-7051, 2023 Cited by PubMed Abstract: The Gram-positive spore-forming bacterium Bacillus anthracis is the causative agent of anthrax, a deadly disease mostly affecting wildlife and livestock, as well as representing a bioterrorism threat. Its cell surface is covered by the mutually exclusive S-layers Sap and EA1, found in early and late growth phases, respectively. Here we report the nanobody-based structural characterization of EA1 and its native lattice contacts. The EA1 assembly domain consists of 6 immunoglobulin-like domains, where three calcium-binding sites structure interdomain contacts that allow monomers to adopt their assembly-competent conformation. Nanobody-induced depolymerization of EA1 S-layers results in surface defects, membrane blebbing and cell lysis under hypotonic conditions, indicating that S-layers provide additional mechanical stability to the cell wall. Taken together, we report a complete model of the EA1 S-layer and present a set of nanobodies that may have therapeutic potential against Bacillus anthracis. PubMed: 37923757DOI: 10.1038/s41467-023-42826-x PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.811 Å) |
Structure validation
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