5VTM
The crystal structure of minor pseudopilin ternary complex of XcpVWX from the Type 2 secretion system of Pseudomonas aeruginosa
Summary for 5VTM
Entry DOI | 10.2210/pdb5vtm/pdb |
Descriptor | Type II secretion system protein J, Type II secretion system protein K, Type II secretion system protein I, ... (5 entities in total) |
Functional Keywords | type 2 secretion system, transport protein |
Biological source | Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1) More |
Total number of polymer chains | 3 |
Total formula weight | 63562.19 |
Authors | |
Primary citation | Zhang, Y.,Faucher, F.,Zhang, W.,Wang, S.,Neville, N.,Poole, K.,Zheng, J.,Jia, Z. Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa. PLoS Pathog., 14:e1007343-e1007343, 2018 Cited by PubMed Abstract: Pseudomonas aeruginosa utilizes the Type II secretion system (T2SS) to translocate a wide range of large, structured protein virulence factors through the periplasm to the extracellular environment for infection. In the T2SS, five pseudopilins assemble into the pseudopilus that acts as a piston to extrude exoproteins out of cells. Through structure determination of the pseudopilin complexes of XcpVWX and XcpVW and function analysis, we have confirmed that two minor pseudopilins, XcpV and XcpW, constitute a core complex indispensable to the pseudopilus tip. The absence of either XcpV or -W resulted in the non-functional T2SS. Our small-angle X-ray scattering experiment for the first time revealed the architecture of the entire pseudopilus tip and established the working model. Based on the interaction interface of complexes, we have developed inhibitory peptides. The structure-based peptides not only disrupted of the XcpVW core complex and the entire pseudopilus tip in vitro but also inhibited the T2SS in vivo. More importantly, these peptides effectively reduced the virulence of P. aeruginosa towards Caenorhabditis elegans. PubMed: 30346996DOI: 10.1371/journal.ppat.1007343 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.041 Å) |
Structure validation
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