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TitleTssK is a trimeric cytoplasmic protein interacting with components of both phage-like and membrane anchoring complexes of the type VI secretion system.
Journal, issue, pagesJ Biol Chem, Vol. 288, Issue 38, Page 27031-27041, Year 2013
Publish dateSep 20, 2013
AuthorsAbdelrahim Zoued / Eric Durand / Cecilia Bebeacua / Yannick R Brunet / Badreddine Douzi / Christian Cambillau / Eric Cascales / Laure Journet /
PubMed AbstractThe Type VI secretion system (T6SS) is a macromolecular machine that mediates bacteria-host or bacteria-bacteria interactions. The T6SS core apparatus assembles from 13 proteins that form two sub- ...The Type VI secretion system (T6SS) is a macromolecular machine that mediates bacteria-host or bacteria-bacteria interactions. The T6SS core apparatus assembles from 13 proteins that form two sub-assemblies: a phage-like complex and a trans-envelope complex. The Hcp, VgrG, TssE, and TssB/C subunits are structurally and functionally related to components of the tail of contractile bacteriophages. This phage-like structure is thought to be anchored to the membrane by a trans-envelope complex composed of the TssJ, TssL, and TssM proteins. However, how the two sub-complexes are connected remains unknown. Here we identify TssK, a protein that establishes contacts with the two T6SS sub-complexes through direct interactions with TssL, Hcp, and TssC. TssK is a cytoplasmic protein assembling trimers that display a three-armed shape, as revealed by TEM and SAXS analyses. Fluorescence microscopy experiments further demonstrate the requirement of TssK for sheath assembly. Our results suggest a central role for TssK by linking both complexes during T6SS assembly.
External linksJ Biol Chem / PubMed:23921384 / PubMed Central
MethodsEM (single particle)
Resolution26.0 Å
Structure data

EMDB-5739:
Electron microscopy map of the T6SS TssK component
Method: EM (single particle) / Resolution: 26.0 Å

Source
  • Escherichia coli (E. coli)

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