5CED
Penicillin G Acylated Bd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus in complex with immunity protein Bd3460
Summary for 5CED
| Entry DOI | 10.2210/pdb5ced/pdb |
| Descriptor | Bd3459, Bd3460, OPEN FORM - PENICILLIN G, ... (4 entities in total) |
| Functional Keywords | transpeptidase and ankyrin repeat, hydrolae, protein binding, hydrolase |
| Biological source | Bdellovibrio bacteriovorus HD100 More |
| Total number of polymer chains | 2 |
| Total formula weight | 74311.28 |
| Authors | Lovering, A.L.,Cadby, I.T.,Lambert, C.,Sockett, R.E. (deposition date: 2015-07-06, release date: 2015-12-09, Last modification date: 2024-11-20) |
| Primary citation | Lambert, C.,Cadby, I.T.,Till, R.,Bui, N.K.,Lerner, T.R.,Hughes, W.S.,Lee, D.J.,Alderwick, L.J.,Vollmer, W.,Sockett, E.R.,Lovering, A.L. Ankyrin-mediated self-protection during cell invasion by the bacterial predator Bdellovibrio bacteriovorus. Nat Commun, 6:8884-8884, 2015 Cited by PubMed Abstract: Predatory Bdellovibrio bacteriovorus are natural antimicrobial organisms, killing other bacteria by whole-cell invasion. Self-protection against prey-metabolizing enzymes is important for the evolution of predation. Initial prey entry involves the predator's peptidoglycan DD-endopeptidases, which decrosslink cell walls and prevent wasteful entry by a second predator. Here we identify and characterize a self-protection protein from B. bacteriovorus, Bd3460, which displays an ankyrin-based fold common to intracellular pathogens of eukaryotes. Co-crystal structures reveal Bd3460 complexation of dual targets, binding a conserved epitope of each of the Bd3459 and Bd0816 endopeptidases. Complexation inhibits endopeptidase activity and cell wall decrosslinking in vitro. Self-protection is vital - ΔBd3460 Bdellovibrio deleteriously decrosslink self-peptidoglycan upon invasion, adopt a round morphology, and lose predatory capacity and cellular integrity. Our analysis provides the first mechanistic examination of self-protection in Bdellovibrio, documents protection-multiplicity for products of two different genomic loci, and reveals an important evolutionary adaptation to an invasive predatory bacterial lifestyle. PubMed: 26626559DOI: 10.1038/ncomms9884 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.02 Å) |
Structure validation
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