ArticleProtein science : a publication of the Protein Society2026
Dynamic interaction of the Yersinia pseudotuberculosis type three secretion system proteins LcrV and LcrG.
Article in Protein science : a publication of the Protein Society, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- From drug export to envelope fitness: characterizing the regulatory landscape of selectiveFrontiers in microbiology · 2026Article
- Dynamic interaction of the Yersinia pseudotuberculosis type three secretion system proteins LcrV and LcrG.Protein science : a publication of the Protein Society · 2026Article
- Glycyrrhizin (GLY) and glycyrrhetinic acid (GA) as potential multi-target antimicrobials: mechanisms, biofilm disruption, and synergy against drug-resistant pathogens.Frontiers in microbiology · 2026Review
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10 authors.
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Abstract
Yersinia pathogenicity is dependent on polarized translocation of effector proteins via the type III secretion system (T3SS). The tip complex situated on the needle structure of the T3SS is required for contact with the eukaryotic host membrane and is to an extent composed of pentameric LcrV. LcrV is a multifunctional protein that also acts as a regulator of the T3SS by virtue of forming a high-affinity complex in the cytoplasm with its chaperone, LcrG. By employing a structure-based approach centered on mass spectrometry, FRET and NMR spectroscopy, we demonstrated that the LcrV-LcrG complex is best described as a multivalent complex, and that the N-terminal domain of LcrV contributes by negatively affecting the LcrG binding affinity. The N-terminal domain of LcrV is dynamic and undergoes a conformational change to accommodate LcrG binding.
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