ArticleActa crystallographica. Section D, Biological crystallography2012
Structure of the cytoplasmic domain of Yersinia pestis YscD, an essential component of the type III secretion system.
Article in Acta crystallographica. Section D, Biological crystallography, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed.
- Type III secretion by Yersinia pseudotuberculosis is reliant upon an authentic N-terminal YscX secretor domain.Molecular microbiology · 2022Article
- The cytoplasmic portion of the T3SS inner membrane ring components sort into distinct families based on biophysical properties.Biochimica et biophysica acta. Proteins and proteomics · 2019Article
- The Structure and Function of Type III Secretion Systems.Microbiology spectrum · 2016Review
- Building a secreting nanomachine: a structural overview of the T3SS.Current opinion in structural biology · 2014Review
- Article
- A refined model of the prototypical Salmonella SPI-1 T3SS basal body reveals the molecular basis for its assembly.PLoS pathogens · 2013Article
- Structure and interactions of the cytoplasmic domain of the Yersinia type III secretion protein YscD.Journal of bacteriology · 2012Article
- Protein export according to schedule: architecture, assembly, and regulation of type III secretion systems from plant- and animal-pathogenic bacteria.Microbiology and molecular biology reviews : MMBR · 2012Review
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3 authors.
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Abstract
The Yersinia pestis YscD protein is an essential component of the type III secretion system. YscD consists of an N-terminal cytoplasmic domain (residues 1-121), a transmembrane linker (122-142) and a large periplasmic domain (143-419). Both the cytoplasmic and the periplasmic domains are required for the assembly of the type III secretion system. Here, the structure of the YscD cytoplasmic domain solved by SAD phasing is presented. Although the three-dimensional structure is similar to those of forkhead-associated (FHA) domains, comparison with the structures of canonical FHA domains revealed that the cytoplasmic domain of YscD lacks the conserved residues that are required for binding phosphothreonine and is therefore unlikely to function as a true FHA domain.
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