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

2n01 is a 2 chain structure with sequence from Xanthomonas citri pv. citri str. 306. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:,
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

Q8PJB3_XANAC

Publication Abstract from PubMed

The 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

  1. Oliveira LC, Souza DP, Oka GU, Lima FD, Oliveira RJ, Favaro DC, Wienk H, Boelens R, Farah CS, Salinas RK. VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System. Structure. 2016 Oct 4;24(10):1707-1718. doi: 10.1016/j.str.2016.07.015. Epub 2016, Sep 1. PMID:27594685 doi:http://dx.doi.org/10.1016/j.str.2016.07.015
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