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TitleCryo-EM reconstruction of Type VI secretion system baseplate and sheath distal end.
Journal, issue, pagesEMBO J, Vol. 37, Issue 4, Year 2018
Publish dateFeb 15, 2018
AuthorsSergey Nazarov / Johannes P Schneider / Maximilian Brackmann / Kenneth N Goldie / Henning Stahlberg / Marek Basler /
PubMed AbstractThe bacterial Type VI secretion system (T6SS) assembles from three major parts: a membrane complex that spans inner and outer membranes, a baseplate, and a sheath-tube polymer. The baseplate ...The bacterial Type VI secretion system (T6SS) assembles from three major parts: a membrane complex that spans inner and outer membranes, a baseplate, and a sheath-tube polymer. The baseplate assembles around a tip complex with associated effectors and connects to the membrane complex by TssK. The baseplate assembly initiates sheath-tube polymerization, which in some organisms requires TssA. Here, we analyzed both ends of isolated non-contractile sheaths by cryo-electron microscopy. Our analysis suggests that the baseplate, solved to an average 8.0 Å resolution, is composed of six subunits of TssE/F/G and the baseplate periphery is decorated by six TssK trimers. The VgrG/PAAR tip complex in the center of the baseplate is surrounded by a cavity, which may accommodate up to ~450 kDa of effector proteins. The distal end of the sheath, resolved to an average 7.5 Å resolution, shows sixfold symmetry; however, its protein composition is unclear. Our structures provide an important step toward an atomic model of the complete T6SS assembly.
External linksEMBO J / PubMed:29255010 / PubMed Central
MethodsEM (single particle)
Resolution7.5 - 8.0 Å
Structure data

EMDB-3878:
The distal end of a non-contractile T6SS sheath.
Method: EM (single particle) / Resolution: 7.5 Å

EMDB-3879:
The baseplate of a non-contractile T6SS sheath.
Method: EM (single particle) / Resolution: 8.0 Å

Source
  • Vibrio cholerae (bacteria)

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