2Y9K
Three-dimensional model of Salmonella's needle complex at subnanometer resolution
Summary for 2Y9K
Entry DOI | 10.2210/pdb2y9k/pdb |
Related | 2Y9J |
EMDB information | 1871 1874 1875 |
Descriptor | PROTEIN INVG (1 entity in total) |
Functional Keywords | protein transport, type iii secretion system, outer membrane ring, secretin family, c15 fold |
Biological source | SALMONELLA ENTERICA SUBSP. ENTERICA SEROVAR TYPHIMURIUM |
Total number of polymer chains | 15 |
Total formula weight | 234253.73 |
Authors | Schraidt, O.,Marlovits, T.C. (deposition date: 2011-02-15, release date: 2011-03-23, Last modification date: 2024-05-08) |
Primary citation | Schraidt, O.,Marlovits, T.C. Three-Dimensional Model of Salmonella'S Needle Complex at Subnanometer Resolution. Science, 331:1192-, 2011 Cited by PubMed Abstract: 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. PubMed: 21385715DOI: 10.1126/SCIENCE.1199358 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (8.3 Å) |
Structure validation
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