4Y7M

T6SS protein TssM C-terminal domain (835-1129) from EAEC

Summary for 4Y7M

• Entry DOI: 10.2210/pdb4y7m/pdb
• Related: 4Y7L
• Descriptor: Hi113 protein, Type VI secretion protein IcmF, SULFATE ION, ... (4 entities in total)
• Functional Keywords: type 6 secretion system, alpha-beta fold, periplasmic protein, membrane protein
• Biological source: Lama glama (Llama); More
• Total number of polymer chains: 4
• Total formula weight: 92933.53

Authors

Nguyen, V.S.,Spinelli, S.,Durand, E.,Roussel, A.,Cambillau, C. (deposition date: 2015-02-15, release date: 2015-08-05, Last modification date: 2024-11-13)

Primary citation

Durand, E.,Nguyen, V.S.,Zoued, A.,Logger, L.,Pehau-Arnaudet, G.,Aschtgen, M.S.,Spinelli, S.,Desmyter, A.,Bardiaux, B.,Dujeancourt, A.,Roussel, A.,Cambillau, C.,Cascales, E.,Fronzes, R.
Biogenesis and structure of a type VI secretion membrane core complex.
Nature, 523:555-560, 2015

PubMed Abstract: 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.

PubMed: 26200339
DOI: 10.1038/nature14667

Experimental method

X-RAY DIFFRACTION (1.92 Å)