Crystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against ....Cell Res. 2013 May;23(5):728-31.

Cell Research, 2013 May;23(5):728-31. doi: 10.1038/cr.2013.53. Epub 2013 Apr 16.

Crystal structure of L,D-transpeptidase LdtMt2 in complex with meropenem reveals the mechanism of carbapenem against Mycobacterium tuberculosis

Li WJ, Li DF, Hu YL, Zhang XE, Bi LJ, Wang DC.

Abstrct

Tuberculosis (TB), an infectious disease caused by the bacillus Mycobacterium tuberculosis, leads to substantial mortality worldwide1. The emergence of multidrug-resistant (MDR) and extensively drug-resistant (XDR) strains of M. tuberculosis has challenged conventional anti-TB therapy and threatens global disease control of TB2,3. The development of new anti-TB drugs is urgently required4. β-lactams are effective antibiotics widely used to treat bacterial infections; however, so far no effective anti-TB antibiotics have emerged from this class of drugs. Previous studies have indicated that an important reason for the lack of effective β-lactam anti-TB antibiotics is the presence of a chromosomally-encoded class A (Ambler) β-lactamase, BlaC, in M. tuberculosis5.

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