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6X65

Legionella pneumophila Dot/Icm T4SS

This is a non-PDB format compatible entry.
Summary for 6X65
Entry DOI10.2210/pdb6x65/pdb
EMDB information22070
DescriptorType IV secretion system unknown protein fragment, DotC, DotD, ... (6 entities in total)
Functional Keywordssecretion, t4ss, dot, protein transport
Biological sourceLegionella pneumophila
More
Total number of polymer chains153
Total formula weight3504416.28
Authors
Durie, C.L.,Sheedlo, M.J.,Chung, J.M.,Byrne, B.G.,Su, M.,Knight, T.,Swanson, M.S.,Lacy, D.B.,Ohi, M.D. (deposition date: 2020-05-27, release date: 2020-10-07, Last modification date: 2024-03-06)
Primary citationDurie, C.L.,Sheedlo, M.J.,Chung, J.M.,Byrne, B.G.,Su, M.,Knight, T.,Swanson, M.,Lacy, D.B.,Ohi, M.D.
Structural analysis of the Legionella pneumophila Dot/Icm type IV secretion system core complex.
Elife, 9:-, 2020
Cited by
PubMed Abstract: is an opportunistic pathogen that causes the potentially fatal pneumonia Legionnaires' Disease. This infection and subsequent pathology require the Dot/Icm Type IV Secretion System (T4SS) to deliver effector proteins into host cells. Compared to prototypical T4SSs, the Dot/Icm assembly is much larger, containing ~27 different components including a core complex reported to be composed of five proteins: DotC, DotD, DotF, DotG, and DotH. Using single particle cryo-electron microscopy (cryo-EM), we report reconstructions of the core complex of the Dot/Icm T4SS that includes a symmetry mismatch between distinct structural features of the outer membrane cap (OMC) and periplasmic ring (PR). We present models of known core complex proteins, DotC, DotD, and DotH, and two structurally similar proteins within the core complex, DotK and Lpg0657. This analysis reveals the stoichiometry and contact interfaces between the key proteins of the Dot/Icm T4SS core complex and provides a framework for understanding a complex molecular machine.
PubMed: 32876045
DOI: 10.7554/eLife.59530
PDB entries with the same primary citation
Experimental method
ELECTRON MICROSCOPY (3.7 Å)
Structure validation

227111

數據於2024-11-06公開中

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