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8G32

Pro-form of a CDCL short from E. anophelis

This is a non-PDB format compatible entry.
Summary for 8G32
Entry DOI10.2210/pdb8g32/pdb
DescriptorThiol-activated cytolysin family protein, SULFATE ION, GLYCEROL, ... (8 entities in total)
Functional Keywordspore-forming toxin, cholesterol-dependent cytolysin like, elizabethkingia anophelis, toxin
Biological sourceElizabethkingia anophelis Ag1
Total number of polymer chains2
Total formula weight79878.01
Authors
Johnstone, B.A.,Christie, M.P.,Morton, C.J.,Parker, M.W. (deposition date: 2023-02-06, release date: 2024-02-07, Last modification date: 2024-06-26)
Primary citationAbrahamsen, H.L.,Sanford, T.C.,Collamore, C.E.,Johnstone, B.A.,Coyne, M.J.,Garcia-Bayona, L.,Christie, M.P.,Evans, J.C.,Farrand, A.J.,Flores, K.,Morton, C.J.,Parker, M.W.,Comstock, L.E.,Tweten, R.K.
Distant relatives of a eukaryotic cell-specific toxin family evolved a complement-like mechanism to kill bacteria.
Nat Commun, 15:5028-5028, 2024
Cited by
PubMed Abstract: Cholesterol-dependent cytolysins (CDCs) comprise a large family of pore-forming toxins produced by Gram-positive bacteria, which are used to attack eukaryotic cells. Here, we functionally characterize a family of 2-component CDC-like (CDCL) toxins produced by the Gram-negative Bacteroidota that form pores by a mechanism only described for the mammalian complement membrane attack complex (MAC). We further show that the Bacteroides CDCLs are not eukaryotic cell toxins like the CDCs, but instead bind to and are proteolytically activated on the surface of closely related species, resulting in pore formation and cell death. The CDCL-producing Bacteroides is protected from the effects of its own CDCL by the presence of a surface lipoprotein that blocks CDCL pore formation. These studies suggest a prevalent mode of bacterial antagonism by a family of two-component CDCLs that function like mammalian MAC and that are wide-spread in the gut microbiota of diverse human populations.
PubMed: 38866748
DOI: 10.1038/s41467-024-49103-5
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (1.85 Å)
Structure validation

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