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2004-05-21
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2004-05-21
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Acta Cryst (2004). D60, 1167-1169 [doi:10.1107/S0907444904009783]
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crystallization papers
Crystallization and preliminary X-ray analysis of [alpha]-isopropylmalate synthase from Mycobacterium tuberculosis
en
[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 A, space group P21 and two molecules in the asymmetric unit. X-ray diffraction data to 2.0 A resolution have been collected.
2004-05-21
International Union of Crystallography
TUBERCULOSIS
BRANCHED-CHAIN AMINO-ACID BIOSYNTHESIS
[ALPHA]-ISOPROPYLMALATE SYNTHASE
STRUCTURAL GENOMICS
Koon, N.
Squire, C.J.
Baker, E.N.
Copyright (c) 2004 International Union of Crystallography
International Union of Crystallography
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