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-Structure paper
Title | Three-dimensional model of Salmonella's needle complex at subnanometer resolution. |
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Journal, issue, pages | Science, Vol. 331, Issue 6021, Page 1192-1195, Year 2011 |
Publish date | Mar 4, 2011 |
Authors | Oliver Schraidt / Thomas C Marlovits / |
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 ...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. |
External links | Science / PubMed:21385715 |
Methods | EM (single particle) |
Resolution | 6.4 - 11.7 Å |
Structure data | EMDB-1871, PDB-2y9k: EMDB-1874: Three-dimensional model of Salmonella's needle complex at subnanometer resolution EMDB-1875: |
Chemicals | ChemComp-HOH: |
Source |
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Keywords | PROTEIN TRANSPORT / TYPE III SECRETION / IR1 / INNER MEMBRANE RING / C24-FOLD / TYPE III SECRETION SYSTEM / OUTER MEMBRANE RING / SECRETIN FAMILY / C15 FOLD |