Journal
SCIENCE
Volume 331, Issue 6021, Pages 1192-1195Publisher
AMER ASSOC ADVANCEMENT SCIENCE
DOI: 10.1126/science.1199358
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- Boehringer Ingelheim Fonds
- Zentrum fur Innovation und Technologie (ZIT)
- Center for Molecular and Cellular Nanostructure Vienna (CMCN)
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Type III secretion systems (T3SSs) are essential virulence factors used by many Gram-negative bacteria to inject proteins that make eukaryotic host cells accessible to invasion. The T3SS core structure, the needle complex (NC), is a similar to 3.5 megadalton-sized, oligomeric, membrane-embedded complex. Analyzing cryo-electron microscopy images of top views of NCs or NC substructures from Salmonella typhimurium revealed a 24-fold symmetry for the inner rings and a 15-fold symmetry for the outer rings, giving an overall C3 symmetry. Local refinement and averaging showed the organization of the central core and allowed us to reconstruct a subnanometer composite structure of the NC, which together with confident docking of atomic structures reveal insights into its overall organization and structural requirements during assembly.
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