Characterization of an oxidoreductase from the arylamine N-acetyltransferase operon in Mycobacterium smegmatis.
Mycobacterium tuberculosis, the most successful bacterial pathogen, causes tuberculosis, a disease that still causes more than 2 million deaths per year. Arylamine N-acetyltransferase is an enzyme that is conserved in most Mycobacterium spp. The nat gene belongs to an operon that is important for the intracellular survival of M. tuberculosis within macrophages. The nat operon in Mycobacterium smegmatis and other fast-growing mycobacterial species has a unique organization containing genes with uncharacterized function. Here, we describe the biochemical, biophysical and structural characterization of the MSMEG_0308 gene product (MS0308) of the M. smegmatis nat operon. While characterizing the function of MS0308, we validated the oxidoreductase property; however, we found that the enzyme was not utilizing dihydrofolate as its substrate, hence we first report that MS0308 is not a dihydrofolate reductase, as annotated in the genome. The structure of this oxidoreductase was solved at 2.0 Å in complex with the cofactor NADPH and has revealed the hydrophobic pocket where the endogenous substrate binds.
|Title:||Characterization of an oxidoreductase from the arylamine N-acetyltransferase operon in Mycobacterium smegmatis.|
|Keywords:||Arylamine N-Acetyltransferase, Crystallography, X-Ray, Humans, Models, Molecular, Mycobacterium smegmatis, NADP, Operon, Oxidoreductases, Recombinant Proteins, Tetrahydrofolate Dehydrogenase|
|UCL classification:||UCL > School of Life and Medical Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences
UCL > School of Life and Medical Sciences > Faculty of Life Sciences > Biosciences (Division of) > Structural and Molecular Biology
UCL > School of Life and Medical Sciences > Faculty of Medical Sciences
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