Figure 3

Comparison of the predicted secondary structure of the murine threonine aldolase protein with that of the crystal structure of threonine aldolase from the bacteria Thermotoga maritima. The labels are: mouse predicted secondary structure, MmTA_PSSM; mouse protein sequence, MmTA_seq; T. maritima protein sequence, TmTA_seq and T. maritima secondary structure 1JG8_ss; alpha-helix, H, highlighted in light blue; beta-sheet, E, highlighted in yellow; c = turn, coil or loop. Identical residues in both proteins are illustrated with a "+" indicating positive equivalence and a "-" a negative equivalence. The PLP-binding lysyl residues are indicated with a pink asterisk and those residues that interact with PLP are indicated with a black asterisk. Those residues that contact the substrates, L-threonine and L-allo-threonine, and the product, glycine, are indicated with a green hash. Residues involved in electrostatic interactions in the catalytic dimer interface are indicated with an ampersand. Residues making contact with calcium ions are indicated with a plus sign and those contacting a chloride ion with a negative sign.