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Helical Structure of the Needle of the Type III Secretion System of Shigella flexneri

Authors :
Frank S. Cordes
Shixin Yang
Kaoru Komoriya
Susan M. Lea
Eric Larquet
Ariel J. Blocker
Edward H. Egelman
Source :
Journal of Biological Chemistry. 278:17103-17107
Publication Year :
2003
Publisher :
Elsevier BV, 2003.

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.

Details

ISSN :
00219258
Volume :
278
Database :
OpenAIRE
Journal :
Journal of Biological Chemistry
Accession number :
edsair.doi.dedup.....9acc4574b628c0f2eef8f34b5fee35d6
Full Text :
https://doi.org/10.1074/jbc.m300091200