7bba

Structure of the TagL peptidoglycan binding domain from EAEC T6SS

spinqualitylabelsall models 7bba, resolution 2.43Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 7bba is a 4 chain structure with sequence from Escherichia coli. This structure supersedes the now removed PDB entry 5m3g. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 2.43Å Ligands: SO4 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function D3GUV9_ECO44 Publication Abstract from PubMed The type VI secretion system (T6SS) is a widespread mechanism of protein delivery into target cells, present in more than a quarter of all sequenced Gram-negative bacteria. The T6SS constitutes an important virulence factor, as it is responsible for targeting effectors in both prokaryotic and eukaryotic cells. The T6SS comprises a tail structure tethered to the cell envelope via a trans-envelope complex. In most T6SS, the membrane complex is anchored to the cell wall by the TagL accessory protein. In this study, we report the first crystal structure of a peptidoglycan-binding domain of TagL. The fold is conserved with members of the OmpA/Pal/MotB family, and more importantly, the peptidoglycan binding site is conserved. This structure further exemplifies how proteins involved in anchoring to the cell wall for different cellular functions rely on an interaction network with peptidoglycan strictly conserved. Anchoring the T6SS to the cell wall: Crystal structure of the peptidoglycan binding domain of the TagL accessory protein.,Nguyen VS, Spinelli S, Cascales E, Roussel A, Cambillau C, Leone P PLoS One. 2021 Jul 2;16(7):e0254232. doi: 10.1371/journal.pone.0254232., eCollection 2021. PMID:34214145 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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