Structural basis for delivery of the intact [Fe2S2] cluster by monothiol glutaredoxin

Biochemistry. 2009 Jul 7;48(26):6041-3. doi: 10.1021/bi900440m.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Catalytic Domain*
  • Escherichia coli Proteins / chemistry*
  • Escherichia coli Proteins / genetics
  • Glutaredoxins / chemistry*
  • Glutaredoxins / genetics
  • Humans
  • Hydrogen Bonding
  • Iron / chemistry*
  • Models, Molecular
  • Molecular Sequence Data
  • Protein Conformation
  • Protein Structure, Secondary
  • Recombinant Proteins / chemistry
  • Sequence Homology, Amino Acid
  • X-Ray Diffraction

Substances

  • Escherichia coli Proteins
  • GLRX2 protein, human
  • Glutaredoxins
  • Recombinant Proteins
  • Iron

Associated data

  • PDB/2WCI_A
  • PDB/2WCI_B