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Monitoring the Assembly of a Secreted Bacterial Virulence Factor Using Site-specific Crosslinking
Published on: December 17, 2013
Identification of the L,D-transpeptidases for peptidoglycan cross-linking in Escherichia coli
Sophie Magnet1, Lionel Dubost, Arul Marie
1INSERM U872-LRMA, Equipe 12, Centre de Recherche des Cordeliers, 15 Rue de l'Ecole de Médecine, 75270 Paris, Cedex 06, France.
Abstract:
Three active-site cysteine L,D-transpeptidases can individually anchor the Braun lipoprotein to the Escherichia coli peptidoglycan. We show here that two additional enzymes of the same family form peptide bonds between the third residues of peptidoglycan stems, generating meso-DAP(3)-->meso-DAP(3) unusual cross-links. This activity partially replaces the D,D-transpeptidase activity of penicillin-binding proteins.
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