The crystal structure of human GLRX5: iron-sulfur cluster co-ordination, tetrameric assembly and monomer activity.
|Abstract||Human GLRX5 (glutaredoxin 5) is an evolutionarily conserved thiol-disulfide oxidoreductase that has a direct role in the maintenance of normal cytosolic and mitochondrial iron homoeostasis, and its expression affects haem biosynthesis and erythropoiesis. We have crystallized the human GLRX5 bound to two [2Fe-2S] clusters and four GSH molecules. The crystal structure revealed a tetrameric organization with the [2Fe-2S] clusters buried in the inter ... [truncated at 450 characters in length]|
|Author||Johansson, Catrine; Roos, Annette K; Montano, Sergio J; et al|
|Subject||Crystallography, X-Ray Disulfides Glutaredoxins Humans Iron-Sulfur Proteins Models, Molecular Oxidation-Reduction Protein Binding Protein Multimerization Protein Structure, Quaternary chemistry metabolism chemistry metabolism chemistry metabolism|