Helical structure of the needle of the type III secretion system of Shigella flexneri.
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 need...
Main Authors: | , , , , , , |
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Format: | Journal article |
Language: | English |
Published: |
2003
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_version_ | 1826266703652192256 |
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author | Cordes, F Komoriya, K Larquet, E Yang, S Egelman, E Blocker, A Lea, S |
author_facet | Cordes, F Komoriya, K Larquet, E Yang, S Egelman, E Blocker, A Lea, S |
author_sort | Cordes, F |
collection | OXFORD |
description | 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. |
first_indexed | 2024-03-06T20:42:59Z |
format | Journal article |
id | oxford-uuid:34e13525-4cc7-4a05-a195-e31412df80d0 |
institution | University of Oxford |
language | English |
last_indexed | 2024-03-06T20:42:59Z |
publishDate | 2003 |
record_format | dspace |
spelling | oxford-uuid:34e13525-4cc7-4a05-a195-e31412df80d02022-03-26T13:28:51ZHelical structure of the needle of the type III secretion system of Shigella flexneri.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:34e13525-4cc7-4a05-a195-e31412df80d0EnglishSymplectic Elements at Oxford2003Cordes, FKomoriya, KLarquet, EYang, SEgelman, EBlocker, ALea, SGram-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. |
spellingShingle | Cordes, F Komoriya, K Larquet, E Yang, S Egelman, E Blocker, A Lea, S Helical structure of the needle of the type III secretion system of Shigella flexneri. |
title | Helical structure of the needle of the type III secretion system of Shigella flexneri. |
title_full | Helical structure of the needle of the type III secretion system of Shigella flexneri. |
title_fullStr | Helical structure of the needle of the type III secretion system of Shigella flexneri. |
title_full_unstemmed | Helical structure of the needle of the type III secretion system of Shigella flexneri. |
title_short | Helical structure of the needle of the type III secretion system of Shigella flexneri. |
title_sort | helical structure of the needle of the type iii secretion system of shigella flexneri |
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