PMID:2006135
| Citation |
Ermler, U and Schulz, GE (1991) The three-dimensional structure of glutathione reductase from Escherichia coli at 3.0 A resolution. Proteins 9:174-9 |
|---|---|
| Abstract |
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). |
| Links |
PubMed Online version:10.1002/prot.340090303 |
| Keywords |
Escherichia coli/enzymology; Escherichia coli/genetics; Glutathione Reductase/chemistry; Glutathione Reductase/genetics; Glutathione Reductase/isolation & purification; Humans; Models, Molecular; Mutagenesis, Site-Directed; Sequence Homology, Nucleic Acid; X-Ray Diffraction |
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