The three‐dimensional structure of glutathione reductase from Escherichia coli 
at 3.0 Å resolution

Ermler, Ulrich; Schulz, Georg E.

doi:10.1002/prot.340090303

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The three‐dimensional structure of glutathione reductase from Escherichia coli at 3.0 Å resolution

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Ermler, U., & Schulz, G. E. (1991). The three‐dimensional structure of glutathione reductase from Escherichia coli at 3.0 Å resolution. Proteins: Structure, Function, and Bioinformatics, 9(3), 174-179. doi:10.1002/prot.340090303.

Cite as: https://hdl.handle.net/21.11116/0000-0008-37E2-B

Abstract

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