Crystallization and preliminary crystallographic analysis of a novel cytochrome P450 from Mycobacterium tuberculosis

Christopher G. Mowat, David Leys, Kirsty J. McLean, Stuart L. Rivers, Alison Richmond, Andrew W. Munro, Miguel Ortiz Lombardia, Pedro M. Alzari, Graeme A. Reid, Stephen K. Chapman, Malcolm D. Walkinshaw

    Research output: Contribution to journalArticlepeer-review

    Abstract

    The product of the Rv2276 gene of Mycobacterium tuberculosis is a cytochrome P450 (P450 MT2, CYP121) which has been shown to bind tightly to a range of azole-based antifungal drugs (e.g. miconazole, clotrimazole). These drugs are potent inhibitors of mycobacterial growth, suggesting that P450 MT2 (CYP121) may be a potential drug target. The enzyme has been overexpressed in Escherichia coli and crystallized by the hanging-drop method. Crystals of P450 MT2 (CYP121) belong to the hexagonal space group P6122 or P6522, with unit-cell parameters a = b = 78.3, c = 265.6 Å. Native data have been collected to 1.6 Å resolution and Hg-derivative data to 2.5 Å resolution using a synchrotron-radiation source.
    Original languageEnglish
    Pages (from-to)704-705
    Number of pages1
    JournalActa Crystallographica Section D: Biological Crystallography
    Volume58
    Issue number4
    DOIs
    Publication statusPublished - 2002

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