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

Christopher Mowat, David Leys, Kirsty McLean, Stuart Rivers, Alison Richmond, Andrew Munro, Miguel Ortiz Lombardia, Pedro Alzari, Graeme Reid, Stephen Chapman, Malcolm 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 pages2
JournalActa Crystallographica Section D: Biological Crystallography
Volume58
DOIs
Publication statusPublished - 2002

Keywords

  • cytochrome
  • P450

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