1. Expression, purification and preliminary crystallographic analysis of Rv3002c, the regulatory subunit of acetolactate synthase (IlvH) fromMycobacterium tuberculosis
- Author
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Jiang Yin, Craig R. Garen, Grace Garen, and Michael N.G. James
- Subjects
Molecular Sequence Data ,Biophysics ,Gene Expression ,Molecular cloning ,Crystallography, X-Ray ,Biochemistry ,Protein Structure, Secondary ,Mycobacterium tuberculosis ,chemistry.chemical_compound ,Biosynthesis ,Structural Biology ,Valine ,Genetics ,Amino Acid Sequence ,health care economics and organizations ,Acetolactate synthase ,Sequence Homology, Amino Acid ,ATP synthase ,biology ,Condensed Matter Physics ,biology.organism_classification ,Acetolactate Synthase ,Protein Subunits ,Crystallography ,chemistry ,Crystallization Communications ,biology.protein ,Isoleucine ,Leucine ,Sequence Alignment - Abstract
Branched amino-acid biosynthesis is important to bacterial pathogens such as Mycobacterium tuberculosis (Mtb), a microorganism that presently causes more deaths in humans than any other prokaryotic pathogen (http://www.who.int/tb). In this study, the molecular cloning, expression, purification, crystallization and preliminary crystallographic analysis of recombinant IlvH, the small regulatory subunit of acetohydroxylic acid synthase (AHAS) in Mtb, are reported. AHAS carries out the first common reaction in the biosynthesis of valine, leucine and isoleucine. AHAS is an essential enzyme in Mtb and its inactivation leads to a lethal phenotype [Sassetti et al. (2001), Proc. Natl Acad. Sci. USA, 98, 12712-12717]. Thus, inhibitors of AHAS could potentially be developed into novel anti-Mtb therapies.
- Published
- 2011