Active site conformational changes upon reaction intermediate biotinyl-5'-AMP binding in biotin protein ligase from Mycobacterium tuberculosis

摘要: Protein biotinylation, a rare form of post-translational modification, is found in enzymes required for lipid biosynthesis. In mycobacteria, this process essential the formation their complex and distinct cell wall has become focal point drug discovery approaches. The enzyme responsible process, biotin protein ligase, substantially varies different species terms overall structural organization, regulation function substrate specificity. To advance understanding molecular mechanism biotinylation Mycobacterium tuberculosis we have biochemically structurally characterized corresponding enzyme. We report high-resolution crystal structures apo-form reaction intermediate biotinyl-5'-AMP-bound M. ligase. Binding leads to clear disorder-to-order transitions. show that conserved lysine, Lys138, active site biotinylation.