Table 1.
Data collection and refinement statistics of the TagL peptidoglycan binding domain (PGBD).
Fig 1.
Sequence alignment of the TagL peptidoglycan binding domain (PGBD) with other representative OmpA family proteins.
Secondary structure elements and numeration from the TagL PGBD structure are displayed above the alignment. Strictly conserved residues are in black blocks; the five residues that were shown to be required for TagL binding to the cell wall are indicated by an asterisk; selected N and C termini of the TagL PGBD are indicated by vertical arrows. 3TD3: OmpA from Acinetobacter baumannii; 4G4X: Pal from Acinetobacter baumannii; 4PWT: Pal from Yersinia pestis. Amino acid sequences were aligned using Multalin [43], and the figure was prepared using ESPript (version 3.0, http://espript.ibcp.fr/) [44].
Fig 2.
Overall structure of the TagL peptidoglycan binding domain (PGBD).
A. The TagL PGBD is displayed as a ribbon diagram with blue β-sheets and red α-helices; the N and C termini are labelled. B. The surface of the TagL PGBD is displayed, with the residues involved in the cell wall binding coloured in red. The figure was prepared using PyMOL (version 1.20, https://pymol.org).
Fig 3.
Superimposition of the TagL peptidoglycan binding domain (PGBD) with other OmpA family proteins in complex with a peptidoglycan (PG) fragment.
Right: TagL PGDB, P. gingivalis PorE (6TOP), A. baumannii Pal (4G4V) and A. baumannii OmpA (3TD4) are displayed in white, cyan, pink and yellow, respectively. The N- and C-terminal extremities are labelled; for clarity purpose the structures are displayed as worm diagram, and only the DAP bound to A. baumannii OmpA is displayed, in stick format. Enclosed: Close-up view of the PG binding site. The PG fragments as well as the side chains of the conserved residues that interact with the DAP residue are displayed in stick format; hydrogen bonds are displayed as dashed lines. For clarity purpose, only the TagL residues are labelled. The figure was prepared using PyMOL (version 1.20, https://pymol.org).