Structure of glutathione reductase from Escherichia coli at 1.86 A resolution: comparison with the enzyme from human erythrocytes.

摘要: The crystal structure of the dimeric flavoenzyme glutathione reductase from Escherichia coli was determined and refined to an R-factor 16.8% at 1.86 A resolution. molecular 2-fold axis dimer is local but very close a possible crystallographic axis; slight asymmetry could be rationalized packing contacts. 2 crystallographically independent subunits are virtually identical, yielding no structural clue on cooperativity. compared with well-known homologous enzyme human erythrocytes 52% sequence identity. Significant differences were found interface, where has disulfide bridge, whereas E. antiparallel beta-sheet connecting subunits. binding site in particular deformation caused by Leu-Ile exchange indicate why accepts trypanothione much better than enzyme. reported provides frame for explaining numerous published engineering results detail guiding further ones.