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Abstract:
An electron density map of the FAD-containing enzyme glutathione reductase from human erythrocytes was produced at 2 Å resolution using the multi-isomorphous-replacement method. The chemically determined amino acid sequence could be fitted unambiguously to this map. The enzyme has a molecular weight of 104,800 and consists of two identical subunits. Each of them can be subdivided into four domains and a flexible segment of 18 residues at the N-terminus. A subunit contains 11 α-helices comprising 31% of all residues and 32% β-structure in five pleated sheets. An intersubunit disulfide bridge, which is not expected for an intracellular enzyme, was detected in the crystal. The heavy atom binding sites, the subunit interface, and the intermolecular contacts in the crystal are discussed.
