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TitleAssembly of the inner rod determines needle length in the type III secretion injectisome.
Journal, issue, pagesNature, Vol. 441, Issue 7093, Page 637-640, Year 2006
Publish dateJun 1, 2006
AuthorsThomas C Marlovits / Tomoko Kubori / María Lara-Tejero / Dennis Thomas / Vinzenz M Unger / Jorge E Galán /
PubMed AbstractAssembly of multi-component supramolecular machines is fundamental to biology, yet in most cases, assembly pathways and their control are poorly understood. An example is the type III secretion ...Assembly of multi-component supramolecular machines is fundamental to biology, yet in most cases, assembly pathways and their control are poorly understood. An example is the type III secretion machine, which mediates the transfer of bacterial virulence proteins into host cells. A central component of this nanomachine is the needle complex or injectisome, an organelle associated with the bacterial envelope that is composed of a multi-ring base, an inner rod, and a protruding needle. Assembly of this organelle proceeds in sequential steps that require the reprogramming of the secretion machine. Here we provide evidence that, in Salmonella typhimurium, completion of the assembly of the inner rod determines the size of the needle substructure. Assembly of the inner rod, which is regulated by the InvJ protein, triggers conformational changes on the cytoplasmic side of the injectisome, reprogramming the secretion apparatus to stop secretion of the needle protein.
External linksNature / PubMed:16738660
MethodsEM (single particle)
Resolution20.0 - 25.0 Å
Structure data

EMDB-1214:
Assembly of the inner rod determines needle length in the type III secretion injectisome.
Method: EM (single particle) / Resolution: 20.0 Å

EMDB-1215:
Assembly of the inner rod determines needle length in the type III secretion injectisome.
Method: EM (single particle) / Resolution: 25.0 Å

Source
  • Salmonella enterica subsp. enterica serovar Typhimurium (bacteria)

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