Structural highlights
Function
[PRGH_SALTY] Required for invasion of epithelial cells. [PRGK_SALTY] Required for invasion of epithelial cells. Could be involved in protein secretion.
Publication Abstract from PubMed
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 ~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.
Three-dimensional model of Salmonella's needle complex at subnanometer resolution.,Schraidt O, Marlovits TC Science. 2011 Mar 4;331(6021):1192-5. PMID:21385715[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Schraidt O, Marlovits TC. Three-dimensional model of Salmonella's needle complex at subnanometer resolution. Science. 2011 Mar 4;331(6021):1192-5. PMID:21385715 doi:10.1126/science.1199358
