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5VTM

The crystal structure of minor pseudopilin ternary complex of XcpVWX from the Type 2 secretion system of Pseudomonas aeruginosa

Summary for 5VTM
Entry DOI10.2210/pdb5vtm/pdb
DescriptorType II secretion system protein J, Type II secretion system protein K, Type II secretion system protein I, ... (5 entities in total)
Functional Keywordstype 2 secretion system, transport protein
Biological sourcePseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)
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Total number of polymer chains3
Total formula weight63562.19
Authors
Zhang, Y.,Jia, Z. (deposition date: 2017-05-17, release date: 2018-05-23, Last modification date: 2023-11-15)
Primary citationZhang, 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: 30346996
DOI: 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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