THE 3-DIMENSIONAL STRUCTURE OF GLUTATHIONE-REDUCTASE FROM ESCHERICHIA-COLI AT 3.0 A RESOLUTION

The structure of glutathione reductase from Escherichia coli has been solved at 3 angstrom resolution using multiple isomorphous replacement, solvent flattening, and molecular replacement on the basis of the homologous (53% identical residues) and structurally well-established human enzyme. The structures of both enzyme species agree with each other in a global way; there is no domain rearrangement In detail, clear structural differences can be observed. The structure analysis of the E. coli enzyme was tackled in order to understand site-directed mutants, the most spectacular of which changed the cofactor specificity of this enzyme from NADP to NAD (Scrutton et al., 1990, Nature 343:38-43).