Deciphering the structural organization of OrfG, the VirB8-like of ICESt3 Type IV secretion system (T4SS)
Résumé
Although predominantly monomeric in solution, the data presented above show that OrfG forms functional trimers in vivo with the same structural organization observed in its crystal structure. Since TraM and TcpC show also the same packing in their crystal structures, this suggests that VirB8-like in Gram+ operate as trimers in their corresponding T4SS. This family of proteins in Gram- bacteria has been a target of choice for the design of conjugation inhibitors. Our study of OrfG structural organization and cellular localization which indicates that the soluble domain of OrfG is located in the cell wall and accessible on the surface of S. thermophilus (data not shown), makes this protein a very interesting target for the design of conjugation inhibitors targeting the trimer contact interfaces.
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