Journal of Structural and Functional Genomics

, Volume 6, Issue 4, pp 245–257

The crystal structure of Rv0793, a hypothetical monooxygenase from M.␣tuberculosis

  • M. Joanne Lemieux
  • Claire Ference
  • Maia M. Cherney
  • Metian Wang
  • Craig Garen
  • Michael N. G. James


Mycobacterium tuberculosis infects millions worldwide. The Structural Genomics Consortium for M. tuberculosis has targeted all genes from this bacterium in hopes of discovering and developing new therapeutic agents. Open reading frame Rv0793 from M. tuberculosis was annotated with an unknown function. The 3-dimensional structure of Rv0793 has been solved to 1.6 Å resolution. Its structure is very similar to that of Streptomyces coelicolor ActVA-Orf6, a monooxygenase that participates in tailoring of polyketide antibiotics in the absence of a cofactor. It is also similar to the recently solved structure of YgiN, a quinol monooxygenase from Escherichia coli. In addition, the structure of Rv0793 is similar to several structures of other proteins with unknown function. These latter structures have been determined recently as a result of structural genomic projects for various bacterial species. In M. tuberculosis, Rv0793 and its homologs may represent a class of monooygenases acting as reactive oxygen species scavengers that are essential for evading host defenses. Since the most prevalent mode of attack by the host defense on M. tuberculosis is by reactive oxygen species and reactive nitrogen species, Rv0793 may provide a novel target to combat infection by M. tuberculosis.

Key words

Mycobacterium tuberculosis, antibiotic biosynthesis monooxygenase quinol monooxygenase X-ray crystallography 


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Supplementary material


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Copyright information

© Springer Science+Business Media, Inc. 2006

Authors and Affiliations

  • M. Joanne Lemieux
    • 1
  • Claire Ference
    • 1
  • Maia M. Cherney
    • 1
  • Metian Wang
    • 2
  • Craig Garen
    • 1
  • Michael N. G. James
    • 1
  1. 1.Department of Biochemistry, CIHR Group in Protein Structure and FunctionUniversity of AlbertaEdmontonCanada
  2. 2.Department of Chemistry and BiochemistryArizona State UniversityTempeUSA

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