1GER

THE STRUCTURE OF GLUTATHIONE REDUCTASE FROM ESCHERICHIA COLI AT 1.86 ANGSTROMS RESOLUTION: COMPARISON WITH THE ENZYME FROM HUMAN ERYTHROCYTES

Summary for 1GER

• Entry DOI: 10.2210/pdb1ger/pdb
• Descriptor: GLUTATHIONE REDUCTASE, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• Functional Keywords: oxidoreductase(flavoenzyme)
• Biological source: Escherichia coli
• Cellular location: Cytoplasm: P06715
• Total number of polymer chains: 2
• Total formula weight: 99227.79

Authors

Mittl, P.R.E.,Schulz, G.E. (deposition date: 1994-01-18, release date: 1994-11-01, Last modification date: 2024-10-23)

Primary citation

Mittl, P.R.,Schulz, G.E.
Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.
Protein Sci., 3:799-809, 1994

PubMed 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.

PubMed: 8061609

Experimental method

X-RAY DIFFRACTION (1.86 Å)