Backbone and side-chain super(1)H, super(15)N and super(13)C assignment of apo- and imipenem-acylated l,d-transpeptidase from Bacillus subtilis

• Published in: Biomolecular NMR assignments 2012-10, Vol.6 (2), p.205-208
• Main Authors: Lecoq, L, Bougault, C, Kern, T, Hugonnet, J-E, Veckerle, C, Pessey, O, Arthur, M, Simorre, J-P
• Format: Article
• Language: English
• Subjects: Bacillus subtilis; Enterococcus faecium; Mycobacterium tuberculosis
• ISSN: 1874-2718; 1874-270X
• DOI: 10.1007/s12104-012-9358-1

The d,d-transpeptidase activity of Penicillin Binding Proteins (PBPs) is essential to maintain cell wall integrity. PBPs catalyze the final step of the peptidoglycan synthesis by forming 4 arrow right 3 cross-links between two peptide stems. Recently, a novel beta -lactam resistance mechanism involving l,d-transpeptidases has been identified in Enterococcus faecium and Mycobacterium tuberculosis. In this resistance pathway, the classical 4 arrow right 3 cross-links are replaced by 3 arrow right 3 cross-links, whose formation are catalyzed by the l,d-transpeptidases. To date, only one class of the entire beta -lactam family, the carbapenems, is able to inhibit the l,d-transpeptidase activity. Nevertheless, the specificity of this inactivation is still not understood. Hence, the study of this new transpeptidase family is of considerable interest in order to understand the mechanism of the l,d-transpeptidases inhibition by carbapenems. In this context, we present herein the backbone and side-chain super(1)H, super(15)N and super(13)C NMR assignment of the l,d-transpeptidase from Bacillus subtilis (Ldt sub(Bs)) in the apo and in the acylated form with a carbapenem, the imipenem.