The three-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 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).
Ermler
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Institut für Organische Chemie und Biochemie, Universität, Freiburg, Federal Republic of Germany.
Schulz
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GE
D004926:Escherichia coli / Q000201:enzymology* / Q000235:genetics; D005980:Glutathione Reductase / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification; D006801:Humans; D008958:Models, Molecular; D016297:Mutagenesis, Site-Directed; D012689:Sequence Homology, Nucleic Acid; D014961:X-Ray Diffraction
D005980:Glutathione Reductase