ArticleActa crystallographica. Section D, Biological crystallography2013
Context-dependent protein folding of a virulence peptide in the bacterial and host environments: structure of an SycH-YopH chaperone-effector complex.
Article in Acta crystallographica. Section D, Biological crystallography, 2013. 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, 15 citations in OpenAlex.
- Class II chaperones: indispensable components of the Gram-negative bacterial T3SS as guardians of translocators.Archives of microbiology · 2026Review
- IDBSpred: An intrinsically disordered binding site predictor using machine learning and protein language model.bioRxiv : the preprint server for biology · 2026Article
- Article
- Identification and analysis of structurally critical fragments in HopS2.BMC bioinformatics · 2019Article
- Molecular basis for CesT recognition of type III secretion effectors in enteropathogenic Escherichia coli.PLoS pathogens · 2018Article
- Molecular basis of binding between the global post-transcriptional regulator CsrA and the T3SS chaperone CesT.Nature communications · 2018Article
- Regulation of Streptococcus mutans PTS Bio by the transcriptional repressor NigR.Molecular oral microbiology · 2015Article
- Structural insight into effector proteins of Gram-negative bacterial pathogens that modulate the phosphoproteome of their host.Protein science : a publication of the Protein Society · 2015Review
- Structure of Salmonella FlhE, conserved member of a flagellar type III secretion operon.Journal of molecular biology · 2015Article
- Type III chaperones & Co in bacterial plant pathogens: a set of specialized bodyguards mediating effector delivery.Frontiers in plant science · 2013Review
- BtcA, A class IA type III chaperone, interacts with the BteA N-terminal domain through a globular/non-globular mechanism.PloS one · 2013Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Yersinia pestis injects numerous bacterial proteins into host cells through an organic nanomachine called the type 3 secretion system. One such substrate is the tyrosine phosphatase YopH, which requires an interaction with a cognate chaperone in order to be effectively injected. Here, the first crystal structure of a SycH-YopH complex is reported, determined to 1.9 Å resolution. The structure reveals the presence of (i) a nonglobular polypeptide in YopH, (ii) a so-called β-motif in YopH and (iii) a conserved hydrophobic patch in SycH that recognizes the β-motif. Biochemical studies establish that the β-motif is critical to the stability of this complex. Finally, since previous work has shown that the N-terminal portion of YopH adopts a globular fold that is functional in the host cell, aspects of how this polypeptide adopts radically different folds in the host and in the bacterial environments are analysed.
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