ArticleActa crystallographica. Section F, Structural biology and crystallization communications2013
Structure of the Yersinia pestis tip protein LcrV refined to 1.65 Å resolution.
Article in Acta crystallographica. Section F, Structural biology and crystallization communications, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers.
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Who cites it
14 citing papers in PubMed.
- Virulence-associated type III secretion systems in Gram-negative bacteria.Microbiology (Reading, England) · 2023Review
- Evolutionary Conservation, Variability, and Adaptation of Type III Secretion Systems.The Journal of membrane biology · 2022Review
- Role of the Yersinia pseudotuberculosis Virulence Plasmid in Pathogen-Phagocyte Interactions in Mesenteric Lymph Nodes.EcoSal Plus · 2021Review
- Interactions between Yersinia pestis V-antigen (LcrV) and human Toll-like receptor 2 (TLR2) in a modelled protein complex and potential mechanistic insights.BMC immunology · 2019Article
- The type III secretion system needle, tip, and translocon.Protein science : a publication of the Protein Society · 2019Review
- On the road to structure-based development of anti-virulence therapeutics targeting the type III secretion system injectisome.MedChemComm · 2019Review
- The Injectisome, a Complex Nanomachine for Protein Injection into Mammalian Cells.EcoSal Plus · 2019Review
- Deoxycholate-Enhanced Shigella Virulence Is Regulated by a Rare π-Helix in the Type Three Secretion System Tip Protein IpaD.Biochemistry · 2017Article
- A Bivalent Anthrax-Plague Vaccine That Can Protect against Two Tier-1 Bioterror Pathogens,Frontiers in immunology · 2017Article
- Characterization of the Binding of Hydroxyindole, Indoleacetic acid, and Morpholinoaniline to the Salmonella Type III Secretion System Proteins SipD and SipB.ChemMedChem · 2016Article
- The Type III Secretion Translocation Pore Senses Host Cell Contact.PLoS pathogens · 2016Article
- The Amino-Terminal Part of the Needle-Tip Translocator LcrV ofFrontiers in cellular and infection microbiology · 2016Article
- The LcrG Tip Chaperone Protein of the Yersinia pestis Type III Secretion System Is Partially Folded.Journal of molecular biology · 2015Article
- Structure of CT584 from Chlamydia trachomatis refined to 3.05 Å resolution.Acta crystallographica. Section F, Structural biology and crystallization communications · 2013Article
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5 authors.
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Abstract
The human pathogen Yersinia pestis requires the assembly of the type III secretion system (T3SS) for virulence. The structural component of the T3SS contains an external needle and a tip complex, which is formed by LcrV in Y. pestis. The structure of an LcrV triple mutant (K40A/D41A/K42A) in a C273S background has previously been reported to 2.2 Å resolution. Here, the crystal structure of LcrV without the triple mutation in a C273S background is reported at a higher resolution of 1.65 Å. Overall the two structures are similar, but there are also notable differences, particularly near the site of the triple mutation. The refined structure revealed a slight shift in the backbone positions of residues Gly28-Asn43 and displayed electron density in the loop region consisting of residues Ile46-Val63, which was disordered in the original structure. In addition, the helical turn region spanning residues Tyr77-Gln95 adopts a different orientation.
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