8ONC
Structure of the C-terminal beta helix domain of the Bdellovibrio bacteriovorus Bd3182 fibre
Summary for 8ONC
| Entry DOI | 10.2210/pdb8onc/pdb |
| Descriptor | Cell wall surface anchor family protein, 1,2-ETHANEDIOL (3 entities in total) |
| Functional Keywords | fibre, adhesin, cell adhesion |
| Biological source | Bdellovibrio bacteriovorus HD100 |
| Total number of polymer chains | 6 |
| Total formula weight | 93176.39 |
| Authors | Caulton, S.G.,Lovering, A.L. (deposition date: 2023-04-01, release date: 2023-10-25, Last modification date: 2024-06-26) |
| Primary citation | Caulton, S.G.,Lambert, C.,Tyson, J.,Radford, P.,Al-Bayati, A.,Greenwood, S.,Banks, E.J.,Clark, C.,Till, R.,Pires, E.,Sockett, R.E.,Lovering, A.L. Bdellovibrio bacteriovorus uses chimeric fibre proteins to recognize and invade a broad range of bacterial hosts. Nat Microbiol, 9:214-227, 2024 Cited by PubMed Abstract: Predatory bacteria, like the model endoperiplasmic bacterium Bdellovibrio bacteriovorus, show several adaptations relevant to their requirements for locating, entering and killing other bacteria. The mechanisms underlying prey recognition and handling remain obscure. Here we use complementary genetic, microscopic and structural methods to address this deficit. During invasion, the B. bacteriovorus protein CpoB concentrates into a vesicular compartment that is deposited into the prey periplasm. Proteomic and structural analyses of vesicle contents reveal several fibre-like proteins, which we name the mosaic adhesive trimer (MAT) superfamily, and show localization on the predator surface before prey encounter. These dynamic proteins indicate a variety of binding capabilities, and we confirm that one MAT member shows specificity for surface glycans from a particular prey. Our study shows that the B. bacteriovorus MAT protein repertoire enables a broad means for the recognition and handling of diverse prey epitopes encountered during bacterial predation and invasion. PubMed: 38177296DOI: 10.1038/s41564-023-01552-2 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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