Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin
Copyright policy )Structural Basis for Delivery of the Intact [Fe2S2] Cluster by Monothiol Glutaredoxin
Glutaredoxins (GRX) are redox proteins which use glutathione as a cofactor and are divided into two classes, monothiol and dithiol. In each class, several GRX have been shown to form [Fe2S2] cluster coordinating homodimers. The dithiol GRX homodimer is proposed to serve as a sequestration form and its iron-sulfur cluster as an oxidative stress sensor. In contrast, the monothiol GRX homodimer has been suggested to act as a scaffold for [Fe2S2] cluster delivery. We present here the structure of a monothiol GRX homodimer (Escherichia coli GRX4) coordinating a [Fe2S2] cluster that reveals the structural basis of intact iron-sulfur cluster delivery.
Models, Molecular, Sequence Homology, Amino Acid, Protein Conformation, Escherichia coli Proteins, Iron, Molecular Sequence Data, Hydrogen Bonding, Protein Structure, Secondary, Recombinant Proteins, X-Ray Diffraction, Catalytic Domain, Humans, Amino Acid Sequence, Glutaredoxins
Models, Molecular, Sequence Homology, Amino Acid, Protein Conformation, Escherichia coli Proteins, Iron, Molecular Sequence Data, Hydrogen Bonding, Protein Structure, Secondary, Recombinant Proteins, X-Ray Diffraction, Catalytic Domain, Humans, Amino Acid Sequence, Glutaredoxins
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