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1: Proteins. 1991;9(3):174-9.Links

The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution.

Ermler U, Schulz GE.

Institut für Organische Chemie und Biochemie, Universität, Freiburg, Federal Republic of Germany.

The structure of glutathione reductase from Escherichia coli has been solved at 3 A 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).

PMID: 2006135 [PubMed - indexed for MEDLINE]