INTERNAL SYMMETRY OF THE TERTIARY STRUCTURE OF NAD-DEPENDENT FORMATE DEHYDROGENASE FROM PSEUDOMONAS SP-101

Comparative 3D analysis was performed on the catalytic and the coenzym e-binding domains of NAD-dependent formate dehydrogenase (FDH). A stru cture of the Rossmann-fold type was revealed in the catalytic domain, and was assessed for homology with the canonical Rossmann folds in FDH and related enzymes. Both FDH domains were found to contain extensive regions comprising a Rossmann fold flanked by two alpha-helices and e xhibiting high 3D homology. FDH proved to have an additional pseudosym metry axis.