Figure 1: Sequence and structure comparisons of MetAPs: Figure 1A. Domain organization of MetAP from E. coli, M. tuberculosis, human MetAPI, human mitochondrial MetAP, rat MetAPII and human MetAPII. K1, K2 and D boxes at the N-termini of MetAPII signify basic and acidic motifs, respectively; the metal binding residues are shown in pink, the highly conserved residues (cyan), Cys (blue), based on the sequence alignment presented in Figure 2. Figure 1B. Divalent metal co-ordination in human MetAPII. Figures 1C and E. Ribbon structure of human MetAPI and two conserved domains with the divalent metal binding site and the NXV motif, PDB 2B3K. Figures 1D and F. Ribbon structure of human MetAPII and two conserved domains with the divalent metal binding site and the disulfide bond, PDB 1BN5. The colors of the residues in the structures are the same as in Figure 1A: His and Met are colored in firebrick and forest, respectively. PyMOL was used for the ribbon drawings.