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.
Iwema
Thomas
T
Laboratoire de Cristallographie et Cristallogenèse des Protéines, Institut de Biologie Structurale Jean-Pierre Ebel, 5075 CEA, CNRS, Universite Joseph Fourier, 41 rue Jules Horowitz, F-38027 Grenoble, France. thomas.iwema@ibs.fr
Picciocchi
Antoine
A
Traore
Daouda A K
DA
Ferrer
Jean-Luc
JL
Chauvat
Franck
F
Jacquamet
Lilian
L
D000595:Amino Acid Sequence; D020134:Catalytic Domain; D029968:Escherichia coli Proteins / Q000737:chemistry* / Q000235:genetics; D054477:Glutaredoxins / Q000737:chemistry* / Q000235:genetics; D006801:Humans; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry*; D008958:Models, Molecular; D008969:Molecular Sequence Data; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D011994:Recombinant Proteins / Q000737:chemistry; D017386:Sequence Homology, Amino Acid; D014961:X-Ray Diffraction
D029968:Escherichia coli Proteins; C516008:GLRX2 protein, human; D054477:Glutaredoxins; D011994:Recombinant Proteins; D007501:Iron