Crystallization and preliminary X-ray analysis of alpha-isopropylmalate synthase from Mycobacterium tuberculosis.
alpha-Isopropylmalate synthase catalyses the aldol condensation of alpha-ketoisovalerate and acetyl coenzyme A to produce alpha-isopropylmalate. This reaction is the first committed step of leucine biosynthesis, which is interrelated with the pathways for production of the other branched-chain amino acids, valine and isoleucine. The absence of these pathways in mammals suggests that these enzymes could be useful targets for drug design against microbial pathogens. The gene for alpha-IPMS in Mycobacterium tuberculosis (Rv3710) has been cloned, expressed in Escherichia coli, both in native and selenomethionine-substituted forms, and crystallized. The SeMet crystals are suitable for high-resolution X-ray structural analysis. These crystals are monoclinic, with unit-cell parameters a = 54.25, b = 154.73, c = 68.82 angstoms, space group P2(1) and two molecules in the asymmetric unit. X-ray diffraction data to 2.0 angstroms resolution have been collected.[1]References
- Crystallization and preliminary X-ray analysis of alpha-isopropylmalate synthase from Mycobacterium tuberculosis. Koon, N., Squire, C.J., Baker, E.N. Acta Crystallogr. D Biol. Crystallogr. (2004) [Pubmed]
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