Figure 1: Contribution of LysM modules (1–6) and linker sequences (L) to the folding and binding activity of the LysM domain.
From: Molecular basis for bacterial peptidoglycan recognition by LysM domains
(a) Domain organization of E. faecalis glucosaminidase AtlA and LysM-derived polypeptides studied. SP, signal peptide; T,E,P-rich, N-terminal domain of unknown function rich in threonine, glutamic acid and proline residues. Amino acid numbers refer to the transition between modules. (b) Sequence alignment of the six LysM modules present in the C-terminal domain of AtlA. Numbering refers to residues corresponding to the LysM module (49 residues); linker sequences are in italics. Identical amino acids in at least four modules are in dark grey boxes, conserved amino acids are in light grey boxes. Secondary structures determined by NMR for 1LysM are indicated. (c) SDS–PAGE of purified recombinant LysM polypeptides described in a; the molecular weight of each purified polypeptide is indicated. (d) Differential scanning calorimetry (DSC) profiles of recombinant LysM polypeptides in the absence (No PG) and presence of peptidoglycan (+PG). Red and dotted blue lines are theoretical curves corresponding to a two-state or a three-state unfolding, respectively. (e) Detection of peptidoglycan binding activities of LysM domains harbouring one to six LysM modules by ELISA.
