2n01
NMR structure of VirB9 C-terminal domain in complex with VirB7 N-terminal domain from Xanthomonas citri's T4SSNMR structure of VirB9 C-terminal domain in complex with VirB7 N-terminal domain from Xanthomonas citri's T4SS
Structural highlights
FunctionPublication Abstract from PubMedThe type IV secretion system (T4SS) from the phytopathogen Xanthomonas citri (Xac) is a bactericidal nanomachine. The T4SS core complex is a ring composed of multiple copies of VirB7-VirB9-VirB10 subunits. Xac-VirB7 contains a disordered N-terminal tail (VirB7NT) that recognizes VirB9, and a C-terminal domain (VirB7CT) involved in VirB7 self-association. Here, we show that VirB7NT forms a short beta strand upon binding to VirB9 and stabilizes it. A tight interaction between them is essential for T4SS assembly and antibacterial activity. Abolishing VirB7 self-association or deletion of the VirB7 C-terminal domain impairs this antibacterial activity without disturbing T4SS assembly. These findings reveal protein interactions within the core complex that are critical for the stability and activity of a T4SS. VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System.,Oliveira LC, Souza DP, Oka GU, Lima FD, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK Structure. 2016 Oct 4;24(10):1707-1718. doi: 10.1016/j.str.2016.07.015. Epub 2016, Sep 1. PMID:27594685[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
|
|