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Binding site‐shaped repeated sequences of bacterial wall peptidoglycan hydrolases
Author(s) -
Ghuysen Jean-Marie,
Lamotte-Brasseur Josette,
Joris Bernard,
Shockman Gerald D.
Publication year - 1994
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(94)80577-6
Subject(s) - peptidoglycan , bacillus subtilis , biochemistry , muramidase , streptomyces albus , amidase , lysozyme , cell wall , amino acid , clostridium acetobutylicum , hydrolase , bacterial cell structure , enzyme , peptide sequence , active site , chemistry , biology , streptomyces , bacteria , gene , butanol , ethanol , genetics
The non‐catalytic C‐terminal regions of the N ‐acetylmuramidase (lysozyme) of Clostridium acetobutylicum and N ‐acetylmuramoyl( d ‐lactyl)‐ l ‐alanine amidases CwlA of Bacillus subtilis , ORFL3 and CwlL of Bacillus licheniformis were previously reported to have similarities with the amino acid sequence of the non‐catalytic N‐terminal module of the Streptomyces albus G Zn DD‐peptidase. This peptidase is a bipartite protein of known three‐dimensional structure. Its non‐catalytic N‐terminal module possesses, exposed at the surface, an elongated crevice which is defined by a loop‐helix‐loop‐helix motif that consists of two repeats, each 16 amino acid residues long, connected by a heptapeptide and whose design is compatible with its possible functioning as a substrate recognition and binding site. Amino acid alignments suggest that cavities nearly identical in shape to that present in the non‐catalytic module of the S. albus peptidase, are borne by the C‐terminal regions of the CwlA amidase (in one copy), the lysozyme and the ORFL3 and CwlL amidases (in two copies). Since a common feature of the five enzymes is their substrate, the bacterial cell wall peptidoglycan, we interpret the striking similarity of their non‐catalytic N‐ or C‐terminal modules to suggest that these modules are involved in the binding of these exocellular enzymes to their insoluble wall substrate.