Helical structure of the needle of the type III secretion system of Shigella flexneri

J Biol Chem. 2003 May 9;278(19):17103-7. doi: 10.1074/jbc.M300091200. Epub 2003 Feb 5.

Abstract

Gram-negative bacteria commonly interact with animal and plant hosts using type III secretion systems (TTSSs) for translocation of proteins into eukaryotic cells during infection. 10 of the 25 TTSS-encoding genes are homologous to components of the bacterial flagellar basal body, which the TTSS needle complex morphologically resembles. This indicates a common ancestry, although no TTSS sequence homologues for the genes encoding the flagellum are found. We here present an approximately 16-A structure of the central component, the needle, of the TTSS. Although the needle subunit is significantly smaller and shares no sequence homology with the flagellar hook and filament, it shares a common helical architecture ( approximately 5.6 subunits/turn, 24-A helical pitch). This common architecture implies that there will be further mechanistic analogies in the functioning of these two bacterial systems.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Bacterial Proteins / chemistry
  • Bacterial Proteins / ultrastructure
  • Flagella / chemistry
  • Gene Expression Regulation, Bacterial
  • Image Processing, Computer-Assisted
  • Protein Conformation
  • Protein Transport*
  • Shigella flexneri / chemistry*
  • Shigella flexneri / ultrastructure

Substances

  • Bacterial Proteins