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- W2157296126 abstract "Significance Secreted pore-forming toxins of pathogenic bacteria such as Escherichia coli and Bordetella pertussis insert into cell membranes to subvert signaling and cause cell death, facilitating infection of human and animal hosts. These toxins require a unique activation step before secretion, the covalent linkage of lipid groups to specific lysines of the inactive protoxin, directed by a specialized toxin-activating acyl transferase (TAAT). Here, we present the TAAT crystal structure, the soluble dimeric topology, and likely active site, revealing that despite no discernible sequence similarity, TAATs are a structurally and functionally distinct group of the Gcn5-like N -acetyl transferase (GNAT) superfamily of modifying enzymes. Our findings open the way to further understanding of the unique toxin activation, and the possibility of inhibiting toxin action." @default.
- W2157296126 created "2016-06-24" @default.
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- W2157296126 date "2015-05-27" @default.
- W2157296126 modified "2023-10-11" @default.
- W2157296126 title "Structure of a bacterial toxin-activating acyltransferase" @default.
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- W2157296126 doi "https://doi.org/10.1073/pnas.1503832112" @default.
- W2157296126 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/4466738" @default.
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