2N01

NMR structure of VirB9 C-terminal domain in complex with VirB7 N-terminal domain from Xanthomonas citri's T4SS

Summary for 2N01

• Entry DOI: 10.2210/pdb2n01/pdb
• Related: 2L4W
• NMR Information: BMRB: 25512
• Descriptor: VirB7 protein, VirB9 protein (2 entities in total)
• Functional Keywords: t4ss, lipoprotein, protein-peptide complex, virb9, virb7, protein transport-protein transport complex, protein transport/protein transport
• Biological source: Xanthomonas axonopodis pv. citri; More
• Total number of polymer chains: 2
• Total formula weight: 15137.03

Authors

Oliveira, L.C.,Souza, D.P.,Salinas, R.K.,Wienk, H.,Boelens, R.,Farah, S.C. (deposition date: 2015-03-03, release date: 2015-09-09, Last modification date: 2024-11-20)

Primary citation

Oliveira, L.C.,Souza, D.P.,Oka, G.U.,Lima, F.D.,Oliveira, R.J.,Favaro, D.C.,Wienk, H.,Boelens, R.,Farah, C.S.,Salinas, R.K.
VirB7 and VirB9 Interactions Are Required for the Assembly and Antibacterial Activity of a Type IV Secretion System.
Structure, 24:1707-1718, 2016

PubMed Abstract: 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 (VirB7) that recognizes VirB9, and a C-terminal domain (VirB7) involved in VirB7 self-association. Here, we show that VirB7 forms a short β 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.

PubMed: 27594685
DOI: 10.1016/j.str.2016.07.015

Experimental method

SOLUTION NMR