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

@article{citeulike:3146506, 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.}, address = {Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom.}, author = {Cordes, F. S. and Komoriya, K. and Larquet, E. and Yang, S. and Egelman, E. H. and Blocker, A. and Lea, S. M.}, citeulike-article-id = {3146506}, citeulike-linkout-0 = {http://dx.doi.org/10.1074/jbc.M300091200}, citeulike-linkout-1 = {http://view.ncbi.nlm.nih.gov/pubmed/12571230}, citeulike-linkout-2 = {http://www.hubmed.org/display.cgi?uids=12571230}, day = {9}, doi = {10.1074/jbc.M300091200}, issn = {0021-9258}, journal = {The Journal of biological chemistry}, keywords = {ttss}, month = {May}, number = {19}, pages = {17103--17107}, posted-at = {2008-08-22 09:48:34}, priority = {0}, title = {Helical structure of the needle of the type III secretion system of Shigella flexneri.}, url = {http://dx.doi.org/10.1074/jbc.M300091200}, volume = {278}, year = {2003} }

TY - JOUR ID - citeulike:3146506 L3 - citeulike-article-id:3146506 N2 - 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. IS - 19 JF - The Journal of biological chemistry SN - 0021-9258 AD - Department of Biochemistry, University of Oxford, South Parks Road, Oxford OX1 3QU, United Kingdom. EP - 17107 TI - Helical structure of the needle of the type III secretion system of Shigella flexneri. VL - 278 SP - 17103 KW - ttss AU - Cordes, FS AU - Komoriya, K AU - Larquet, E AU - Yang, S AU - Egelman, EH AU - Blocker, A AU - Lea, SM PY - 2003/05/09/ UR - http://dx.doi.org/10.1074/jbc.M300091200 ER -