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Structure of a tripartite protein complex that targets toxins to the type VII secretion system

Proc Natl Acad Sci U S A. 2024-01; 
Timothy A Klein, Prakhar Y Shah, Polyniki Gkragkopoulou, Dirk W Grebenc, Youngchang Kim, John C Whitney
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Proteins, Expression, Isolation and Analysis … This complex was purified in PBS pH 7.4 and yielded 10 mg of total protein that was subsequently shipped to Genscript for custom antibody production. The generation of the α-TelC … Get A Quote

摘要

Type VII secretion systems are membrane-embedded nanomachines used by Gram-positive bacteria to export effector proteins from the cytoplasm to the extracellular environment. Many of these effectors are polymorphic toxins comprised of an N-terminal Leu-x-Gly (LXG) domain of unknown function and a C-terminal toxin domain that inhibits the growth of bacterial competitors. In recent work, it was shown that LXG effectors require two cognate Lap proteins for T7SS-dependent export. Here, we present the 2.6 ? structure of the LXG domain of the TelA toxin from the opportunistic pathogen in complex with both of its cognate Lap targeting factors. The structure reveals an elongated α-helical bundle within which each Lap... More

關鍵詞

bacterial secretion systems, bacterial toxins, protein biochemistry, protein export, structural biology
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