PMID:8061609
| Citation |
Mittl, PR and Schulz, GE (1994) Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes. Protein Sci. 3:799-809 |
|---|---|
| Abstract |
The crystal structure of the dimeric flavoenzyme glutathione reductase from Escherichia coli was determined and refined to an R-factor of 16.8% at 1.86 A resolution. The molecular 2-fold axis of the dimer is local but very close to a possible crystallographic 2-fold axis; the slight asymmetry could be rationalized from the packing contacts. The 2 crystallographically independent subunits of the dimer are virtually identical, yielding no structural clue on possible cooperativity. The structure was compared with the well-known structure of the homologous enzyme from human erythrocytes with 52% sequence identity. Significant differences were found at the dimer interface, where the human enzyme has a disulfide bridge, whereas the E. coli enzyme has an antiparallel beta-sheet connecting the subunits. The differences at the glutathione binding site and in particular a deformation caused by a Leu-Ile exchange indicate why the E. coli enzyme accepts trypanothione much better than the human enzyme. The reported structure provides a frame for explaining numerous published engineering results in detail and for guiding further ones. |
| Links |
PubMed PMC2142722 Online version:10.1002/pro.5560030509 |
| Keywords |
Amino Acid Sequence; Binding Sites; Crystallization; Crystallography, X-Ray; Erythrocytes/enzymology; Escherichia coli/enzymology; Escherichia coli/genetics; Glutathione Reductase/blood; Glutathione Reductase/chemistry; Glutathione Reductase/genetics; Humans; Models, Molecular; Molecular Sequence Data; Molecular Structure; Protein Conformation; Protein Structure, Secondary; Solvents; Species Specificity; Water/chemistry |
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