Structural basis for recognition of the type VI spike protein VgrG3 by a cognate immunity protein

AbstractThe bacterial type VI secretion system (T6SS) is used by donor cells to inject toxic effectors into receptor cells. The donor cells produce the corresponding immunity proteins to protect themselves against the effector proteins, thereby preventing their self-intoxication. Recently, the C-terminal domain of VgrG3 was identified as a T6SS effector. Information on the molecular mechanism of VgrG3 and its immunity protein TsaB has been lacking. Here, we determined the crystal structures of native TsaB and the VgrG3C–TsaB complex. VgrG3C adopts a canonical phage-T4-lysozyme-like fold. TsaB interacts with VgrG3C through molecular mimicry, and inserts into the VgrG3C pocket.Structured summary of protein interactionsVgrG3 and TsaB bind by x-ray crystallography (View interaction)TsaB and TsaB bind by x-ray crystallography (View interaction)VgrG3 and TsaB bind by cosedimentation in solution (View interaction)TsaB and TsaB bind by cosedimentation in solution (1,2)TsaB binds to VgrG3 by surface plasmon resonance (1, 2, 3, 4, 5, 6, 7)VgrG3 and TsaB bind by molecular sieving (View interaction)TsaB and TsaB bind by molecular sieving (View interaction)VgrG3 and TsaB bind by x ray scattering (View interaction