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

FS Cordes, K Komoriya, E Larquet, S Yang, EH Egelman, AJ Blocker, SM Lea

Research output: Contribution to journalArticle (Academic Journal)peer-review

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.
Translated title of the contributionHelical structure of the needle of the type III secretion system of Shigella flexneri
Original languageEnglish
Pages (from-to)17103 - 17107
JournalJournal of Biological Chemistry
Volume278
Publication statusPublished - 2003

Bibliographical note

Other identifier: PMID: 12571230

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