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-Structure paper
タイトル | Three-dimensional reconstruction of the Shigella T3SS transmembrane regions reveals 12-fold symmetry and novel features throughout. |
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ジャーナル・号・ページ | Nat Struct Mol Biol, Vol. 16, Issue 5, Page 477-485, Year 2009 |
掲載日 | 2009年4月26日 |
![]() | Julie L Hodgkinson / Ashley Horsley / David Stabat / Martha Simon / Steven Johnson / Paula C A da Fonseca / Edward P Morris / Joseph S Wall / Susan M Lea / Ariel J Blocker / ![]() |
PubMed 要旨 | Type III secretion systems (T3SSs) mediate bacterial protein translocation into eukaryotic cells, a process essential for virulence of many Gram-negative pathogens. They are composed of a cytoplasmic ...Type III secretion systems (T3SSs) mediate bacterial protein translocation into eukaryotic cells, a process essential for virulence of many Gram-negative pathogens. They are composed of a cytoplasmic secretion machinery and a base that bridges both bacterial membranes, into which a hollow, external needle is embedded. When isolated, the latter two parts are termed the 'needle complex'. An incomplete understanding of the structure of the needle complex has hampered studies of T3SS function. To estimate the stoichiometry of its components, we measured the mass of its subdomains by scanning transmission electron microscopy (STEM). We determined subunit symmetries by analysis of top and side views within negatively stained samples in low-dose transmission electron microscopy (TEM). Application of 12-fold symmetry allowed generation of a 21-25-A resolution, three-dimensional reconstruction of the needle complex base, revealing many new features and permitting tentative docking of the crystal structure of EscJ, an inner membrane component. |
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手法 | EM (単粒子) |
解像度 | 25.0 Å |
構造データ | ![]() EMDB-1617: |
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