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PDBsum entry 5cea
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Protein binding
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PDB id
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5cea
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References listed in PDB file
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Key reference
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Title
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Ankyrin-Mediated self-Protection during cell invasion by the bacterial predator bdellovibrio bacteriovorus.
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Authors
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C.Lambert,
I.T.Cadby,
R.Till,
N.K.Bui,
T.R.Lerner,
W.S.Hughes,
D.J.Lee,
L.J.Alderwick,
W.Vollmer,
R.E.Sockett,
E.R.Sockett,
A.L.Lovering.
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Ref.
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Nat Commun, 2015,
6,
8884.
[DOI no: ]
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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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.
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