Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition
(2014) Structure — Vol. 22, n° 7, p. 949-960 (2014)
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- Peptidoglycan surrounds the bacterial cytoplasmic membrane to protect the cell against osmolysis. The biosynthesis of peptidoglycan, made of glycan strands crosslinked by short peptides, is the target of antibiotics like β-lactams and glycopeptides. Nascent peptidoglycan contains pentapeptides that are trimmed by carboxypeptidases to tetra- and tripeptides. The well-characterized DD-carboxypeptidases hydrolyze the terminal D-alanine from the stem pentapeptide to produce a tetrapeptide. However, few LD-carboxypeptidases that produce tripeptides have been identified, and nothing is known about substrate specificity in these enzymes. We report biochemical properties and crystal structures of the LD-carboxypeptidases LdcB from Streptococcus pneumoniae, Bacillus anthracis, and Bacillus subtilis. The enzymes are active against bacterial cell wall tetrapeptides and adopt a zinc-carboxypeptidase fold characteristic of the LAS superfamily. We have also solved the structure of S. pneumoniae LdcB with a product mimic, elucidating the residues essential for peptidoglycan recognition and the conformational changes that occur on ligand binding. © 2014 The Authors.
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Hoyland, C. N., Lewis, R. J., Vollmer, W., Savchenko, A., Daniel, R. A., Anderson, W. F., Stogios, P. J., Sidiq, K., Onopriyenko, O., Minasov, G., Duchêne, M.-C., Cleverley, R. M., & Aldridge, C. (2014). Structure of the LdcB LD-carboxypeptidase reveals the molecular basis of peptidoglycan recognition. Structure, 22(7), 949-960. https://doi.org/10.1016/j.str.2014.04.015 (Original work published 2014)