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The l,d-transpeptidases (Ldts) are promising antibiotic targets for treating tuberculosis. We report screening of cysteine-reactive inhibitors against LdtMt2 from Mycobacterium tuberculosis. Structural studies on LdtMt2 with potent inhibitor ebselen reveal opening of the benzisoselenazolone ring by a nucleophilic cysteine, forming a complex involving extensive hydrophobic interactions with a substrate-binding loop.

Original publication

DOI

10.1039/c9cc04145a

Type

Journal article

Journal

Chem Commun (Camb)

Publication Date

22/08/2019

Volume

55

Pages

10214 - 10217

Keywords

Antitubercular Agents, Azoles, Benzene Derivatives, Cysteine, Enzyme Inhibitors, Humans, Isoindoles, Molecular Docking Simulation, Mycobacterium tuberculosis, Organoselenium Compounds, Peptidyl Transferases, Tuberculosis