Common and distinct structural features of Salmonella injectisome and flagellar basal body

• Published in: Scientific reports 2013-11, Vol.3 (1), p.3369-3369, Article 3369
• Main Authors: Kawamoto, Akihiro, Morimoto, Yusuke V., Miyata, Tomoko, Minamino, Tohru, Hughes, Kelly T., Kato, Takayuki, Namba, Keiichi
• Format: Article
• Language: English
• Subjects: 101/28; 14; 14/63; 631/326/1320; 631/535/1258/1260; Adenosine triphosphatase; Adenosine Triphosphatases - metabolism; Bacterial Proteins - metabolism; Basal Bodies - metabolism; Cryoelectron Microscopy - methods; Crystal structure; Flagella; Flagella - metabolism; Humanities and Social Sciences; multidisciplinary; Protein Transport - physiology; Salmonella; Salmonella - metabolism; Science; Secretion; Self-assembly; Virulence; Virulence - physiology
• ISSN: 2045-2322; 2045-2322
• DOI: 10.1038/srep03369

Bacterial pathogens use an injectisome to deliver virulence proteins into eukaryotic host cells. The bacterial flagellum and injectisome export their component proteins for self-assembly. These two systems show high structural similarities and are classified as the type III secretion system, but it remains elusive how similar they are in situ because the structures of these complexes isolated from cells and visualized by electron cryomicroscopy have shown only the export channel and housing for the export apparatus. Here we report in situ structures of Salmonella injectisome and flagellum by electron cryotomography. The injectisome lacks the flagellar basal body C-ring, but a wing-like disc and a globular density corresponding to the export gate platform and ATPase hexamer ring, respectively, are stably attached through thin connectors, revealing yet unidentified common architectures of the two systems. The ATPase ring is far from the disc, suggesting that both apparatuses are observed in an export-off state.