7O21
Structure of Bdellovibrio bacteriovorus Bd1075
Summary for 7O21
| Entry DOI | 10.2210/pdb7o21/pdb |
| Descriptor | Uncharacterized conserved, BROMIDE ION, THIOCYANATE ION, ... (6 entities in total) |
| Functional Keywords | peptidoglycan ld-carboxypeptidase ntf2, hydrolase |
| Biological source | Bdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100) |
| Total number of polymer chains | 2 |
| Total formula weight | 76787.37 |
| Authors | Lovering, A.L.,Valdivia-Delgado, M. (deposition date: 2021-03-30, release date: 2021-04-21, Last modification date: 2024-06-19) |
| Primary citation | Banks, E.J.,Valdivia-Delgado, M.,Biboy, J.,Wilson, A.,Cadby, I.T.,Vollmer, W.,Lambert, C.,Lovering, A.L.,Sockett, R.E. Asymmetric peptidoglycan editing generates cell curvature in Bdellovibrio predatory bacteria. Nat Commun, 13:1509-1509, 2022 Cited by PubMed Abstract: Peptidoglycan hydrolases contribute to the generation of helical cell shape in Campylobacter and Helicobacter bacteria, while cytoskeletal or periskeletal proteins determine the curved, vibrioid cell shape of Caulobacter and Vibrio. Here, we identify a peptidoglycan hydrolase in the vibrioid-shaped predatory bacterium Bdellovibrio bacteriovorus which invades and replicates within the periplasm of Gram-negative prey bacteria. The protein, Bd1075, generates cell curvature in B. bacteriovorus by exerting LD-carboxypeptidase activity upon the predator cell wall as it grows inside spherical prey. Bd1075 localizes to the outer convex face of B. bacteriovorus; this asymmetric localization requires a nuclear transport factor 2-like (NTF2) domain at the protein C-terminus. We solve the crystal structure of Bd1075, which is monomeric with key differences to other LD-carboxypeptidases. Rod-shaped Δbd1075 mutants invade prey more slowly than curved wild-type predators and stretch invaded prey from within. We therefore propose that the vibrioid shape of B. bacteriovorus contributes to predatory fitness. PubMed: 35314810DOI: 10.1038/s41467-022-29007-y PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.34 Å) |
Structure validation
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