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The fatty acid elongation system FAS-II is involved in the biosynthesis of mycolic acids, which are major and specific long chain fatty acids of the cell envelope of Mycobacterium tuberculosis and other mycobacteria, including M. smegmatis . The protein MabA, also named FabG1, has recently been shown to be part of FAS-II and to catalyse the NADPH-specific reduction of long chain beta-ketoacyl derivatives. This activity corresponds to the second step of a FAS-II elongation round. FAS-II is inhibited by the antituberculous drug isoniazid. Thus, the other enzymes making up this enzymatic complex represent potential targets for designing new antituberculous drugs. We first solved the crystal structure at 2.0 Å resolution of the wild-type apo-enzyme. After examination of the sequence of MabA and its homologue we performed various mutations. The structure activity relationship was studies by the way of these mutants' structures

acta crystallographica. section a, foundations of crystallography/acta crystallographica. section a

Structure function activity studies regarding of the crystal structures of the protein MabA wild type and mutants from<i>Mycobacterium tuberculosis</i>

Structure function activity studies regarding of the crystal structures of the protein MabA wild type and mutants fromMycobacterium tuberculosis