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5CEB

Bd3459 Predatory Endopeptidase from Bdellovibrio bacteriovorus, K38M form

Summary for 5CEB
Entry DOI10.2210/pdb5ceb/pdb
DescriptorBd3459 (2 entities in total)
Functional Keywordstranspeptidase, hydrolase
Biological sourceBdellovibrio bacteriovorus (strain ATCC 15356 / DSM 50701 / NCIB 9529 / HD100)
Total number of polymer chains2
Total formula weight98406.81
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: 2024-11-13)
Primary citationLambert, 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: 26626559
DOI: 10.1038/ncomms9884
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.93 Å)
Structure validation

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数据于2025-06-18公开中

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