ArticleActa crystallographica. Section D, Biological crystallography2011
Structure of the minor pseudopilin XcpW from the Pseudomonas aeruginosa type II secretion system.
Article in Acta crystallographica. Section D, Biological crystallography, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed, 17 citations in OpenAlex.
- Secretory System Components as Potential Prophylactic Targets for Bacterial Pathogens.Biomolecules · 2021Review
- In Situ Proteolysis Condition-Induced Crystallization of the XcpVWX Complex in Different Lattices.International journal of molecular sciences · 2020Article
- Sequence analysis and confirmation of the type IV pili-associated proteins PilY1, PilW and PilV in Acidithiobacillus thiooxidans.PloS one · 2019Article
- Structure-guided disruption of the pseudopilus tip complex inhibits the Type II secretion in Pseudomonas aeruginosa.PLoS pathogens · 2018Article
- Structures of type IV pilins from Thermus thermophilus demonstrate similarities with type II secretion system pseudopilins.Journal of structural biology · 2016Article
- Crystal Structure of the Minor Pilin CofB, the Initiator of CFA/III Pilus Assembly in Enterotoxigenic Escherichia coli.The Journal of biological chemistry · 2015Article
- High-resolution structure of a type IV pilin from the metal-reducing bacterium Shewanella oneidensis.BMC structural biology · 2015Article
- On the path to uncover the bacterial type II secretion system.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2012Review
- The type II secretion system: biogenesis, molecular architecture and mechanism.Nature reviews. Microbiology · 2012Review
- Structural insights into the Type II secretion nanomachine.Current opinion in structural biology · 2012Review
- Ultrahigh resolution and full-length pilin structures with insights for filament assembly, pathogenic functions, and vaccine potential.The Journal of biological chemistry · 2011Article
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Authors and funding
6 authors at 4 institutions in 3 countries.
Funding
Abstract
Pseudomonas aeruginosa utilizes the type II secretion machinery to transport virulence factors through the outer membrane into the extracellular space. Five proteins in the type II secretion system share sequence homology with pilin subunits of type IV pili and are called the pseudopilins. The major pseudopilin XcpT(G) assembles into an intraperiplasmic pilus and is thought to act in a piston-like manner to push substrates through an outer membrane secretin. The other four minor pseudopilins, XcpU(H), XcpV(I), XcpW(J) and XcpX(K), play less well defined roles in pseudopilus formation. It was recently discovered that these four minor pseudopilins form a quaternary complex that is presumed to initiate the formation of the pseudopilus and to localize to its tip. Here, the structure of XcpW(J) was refined to 1.85 Å resolution. The structure revealed the type IVa pilin fold with an embellished variable antiparallel β-sheet as also found in the XcpW(J) homologue enterotoxigenic Escherichia coli GspJ(W) and the XcpU(H) homologue Vibrio cholerae EpsU(H). It is proposed that the exposed surface of this sheet may cradle the long N-terminal α1 helix of another pseudopilin. The final 31 amino acids of the XcpW(J) structure are instrinsically disordered. Deletion of this unstructured region of XcpW(J) did not prevent type II secretion in vivo.
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