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TitleBiogenesis and structure of a type VI secretion membrane core complex.
Journal, issue, pagesNature, Vol. 523, Issue 7562, Page 555-560, Year 2015
Publish dateJul 30, 2015
AuthorsEric Durand / Van Son Nguyen / Abdelrahim Zoued / Laureen Logger / Gérard Péhau-Arnaudet / Marie-Stéphanie Aschtgen / Silvia Spinelli / Aline Desmyter / Benjamin Bardiaux / Annick Dujeancourt / Alain Roussel / Christian Cambillau / Eric Cascales / Rémi Fronzes /
PubMed AbstractBacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence ...Bacteria share their ecological niches with other microbes. The bacterial type VI secretion system is one of the key players in microbial competition, as well as being an important virulence determinant during bacterial infections. It assembles a nano-crossbow-like structure in the cytoplasm of the attacker cell that propels an arrow made of a haemolysin co-regulated protein (Hcp) tube and a valine-glycine repeat protein G (VgrG) spike and punctures the prey's cell wall. The nano-crossbow is stably anchored to the cell envelope of the attacker by a membrane core complex. Here we show that this complex is assembled by the sequential addition of three type VI subunits (Tss)-TssJ, TssM and TssL-and present a structure of the fully assembled complex at 11.6 Å resolution, determined by negative-stain electron microscopy. With overall C5 symmetry, this 1.7-megadalton complex comprises a large base in the cytoplasm. It extends in the periplasm via ten arches to form a double-ring structure containing the carboxy-terminal domain of TssM (TssMct) and TssJ that is anchored in the outer membrane. The crystal structure of the TssMct-TssJ complex coupled to whole-cell accessibility studies suggest that large conformational changes induce transient pore formation in the outer membrane, allowing passage of the attacking Hcp tube/VgrG spike.
External linksNature / PubMed:26200339
MethodsEM (single particle) / X-ray diffraction
Resolution1.51 - 11.5 Å
Structure data

EMDB-2927:
Negative stain structure of a type 6 secretion system membrane core complex
Method: EM (single particle) / Resolution: 11.5 Å

EMDB-2928:
Negative stain structure of a type 6 secretion system membrane core complex
Method: EM (single particle) / Resolution: 11.5 Å

PDB-4y7l:
T6SS protein TssM C-terminal domain (869-1107) from EAEC
Method: X-RAY DIFFRACTION / Resolution: 1.51 Å

PDB-4y7m:
T6SS protein TssM C-terminal domain (835-1129) from EAEC
Method: X-RAY DIFFRACTION / Resolution: 1.92 Å

PDB-4y7o:
T6SS protein TssM C-terminal domain (869-1107) from EAEC
Method: X-RAY DIFFRACTION / Resolution: 2.24 Å

Chemicals

ChemComp-GOL:
GLYCEROL / Glycerol

ChemComp-ZN:
Unknown entry

ChemComp-HOH:
WATER / Water

ChemComp-SO4:
SULFATE ION / Sulfate

Source
  • Escherichia coli (strain 55989 / EAEC) (bacteria)
  • escherichia coli 2-156-04_s3_c3 (bacteria)
  • lama glama (llama)
  • escherichia coli 1-176-05_s3_c1 (bacteria)
  • escherichia coli (E. coli)
KeywordsMEMBRANE PROTEIN / Type 6 secretion system / Alpha-beta fold / periplasmic protein / SIGNALING PROTEIN

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