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Helical Structure of the Needle of the Type III Secretion System of Shigella flexneri
- 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.
- Subjects :
- Genetics
biology
Protein Conformation
Protein subunit
Gene Expression Regulation, Bacterial
Cell Biology
biochemical phenomena, metabolism, and nutrition
Flagellum
biology.organism_classification
Biochemistry
Shigella flexneri
Type three secretion system
Transport protein
Protein Transport
Protein structure
Bacterial Proteins
Flagella
Image Processing, Computer-Assisted
Secretion
Molecular Biology
Gene
Subjects
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