The unusual binding mode of cnicin to the antibacterial target enzyme MurA revealed by X-ray crystallography.

J. Med. Chem.2008 Aug 28;51(16):5143-7. doi:10.1021/jm800609p. Epub 2008 Aug 01

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We present the X-ray structure of the antibacterial target enzyme MurA in complex with its substrate UNAG and the sesquiterpene lactone cnicin, a potent inhibitor of the enzyme. The structure reveals that MurA has catalyzed the formation of a covalent adduct between cnicin and UNAG. This adduct, which can be regarded as a noncovalent suicide inhibitor, has been formed by an unusual "anti-Michael" 1,3-addition of UNAG to an alpha,beta-unsaturated carbonyl function in cnicin.

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The unusual binding mode of cnicin to the antibacterial target enzyme MurA revealed by X-ray crystallography.

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