Document Detail

Backbone and side-chain (1)H, (15)N and (13)C assignment of apo- and imipenem-acylated L: ,D: -transpeptidase from Bacillus subtilis.
MedLine Citation:
PMID:  22278298     Owner:  NLM     Status:  Publisher    
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 → 3 cross-links between two peptide stems. Recently, a novel β-lactam resistance mechanism involving L: ,D: -transpeptidases has been identified in Enterococcus faecium and Mycobacterium tuberculosis. In this resistance pathway, the classical 4 → 3 cross-links are replaced by 3 → 3 cross-links, whose formation are catalyzed by the L: ,D: -transpeptidases. To date, only one class of the entire β-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 (1)H, (15)N and (13)C NMR assignment of the L: ,D: -transpeptidase from Bacillus subtilis (Ldt(Bs)) in the apo and in the acylated form with a carbapenem, the imipenem.
L Lecoq; C Bougault; T Kern; J-E Hugonnet; C Veckerlé; O Pessey; M Arthur; J-P Simorre
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Publication Detail:
Type:  JOURNAL ARTICLE     Date:  2012-1-26
Journal Detail:
Title:  Biomolecular NMR assignments     Volume:  -     ISSN:  1874-270X     ISO Abbreviation:  -     Publication Date:  2012 Jan 
Date Detail:
Created Date:  2012-1-26     Completed Date:  -     Revised Date:  -    
Medline Journal Info:
Nlm Unique ID:  101472371     Medline TA:  Biomol NMR Assign     Country:  -    
Other Details:
Languages:  ENG     Pagination:  -     Citation Subset:  -    
CEA, Institut de Biologie Structurale Jean-Pierre Ebel, 41, rue Jules Horowitz, 38027, Grenoble, France.
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