6ski

The Tle hydrolase bound to the TTR domain of the VgrG spike of the Type 6 secretion system

spinqualitylabelsall models 6ski, resolution 2.60Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 6ski is a 2 chain structure with sequence from Escherichia coli. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: Electron Microscopy, Resolution 2.6Å Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function A0A377LA80_ECOLX Publication Abstract from PubMed The bacterial type VI secretion system (T6SS) is a macromolecular machine that injects effectors into prokaryotic and eukaryotic cells. The mode of action of the T6SS is similar to contractile phages: the contraction of a sheath structure pushes a tube topped by a spike into target cells. Effectors are loaded onto the spike or confined into the tube. In enteroaggregative Escherichia coli, the Tle1 phospholipase binds the C-terminal extension of the VgrG trimeric spike. Here, we purify the VgrG-Tle1 complex and show that a VgrG trimer binds three Tle1 monomers and inhibits their activity. Using covalent cross-linking coupled to high-resolution mass spectrometry, we provide information on the sites of contact and further identify the requirement for a Tle1 N-terminal secretion sequence in complex formation. Finally, we report the 2.6-A-resolution cryo-electron microscopy tri-dimensional structure of the (VgrG)3 -(Tle1)3 complex revealing how the effector binds its cargo, and how VgrG inhibits Tle1 phospholipase activity. The inhibition of Tle1 phospholipase activity once bound to VgrG suggests that Tle1 dissociation from VgrG is required upon delivery. Structural basis for loading and inhibition of a bacterial T6SS phospholipase effector by the VgrG spike.,Flaugnatti N, Rapisarda C, Rey M, Beauvois SG, Nguyen VA, Canaan S, Durand E, Chamot-Rooke J, Cascales E, Fronzes R, Journet L EMBO J. 2020 Jun 2;39(11):e104129. doi: 10.15252/embj.2019104129. Epub 2020 Apr, 30. PMID:32350888 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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