A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters

Chem Commun (Camb). 2014 Apr 14;50(29):3795-8. doi: 10.1039/c3cc48239a.

Abstract

Glutathione-complexed [2Fe-2S] cluster is shown to significantly stimulate the ATPase activity of an ABCB7-type transporter in both solution and proteoliposome-bound forms (KD ∼ 68 μM). The cluster is a likely natural substrate for this transporter, which has been implicated in cytosolic Fe-S cluster protein maturation. A possible substrate-binding site is identified on a new structural model for the active transporter.

Publication types

  • Research Support, N.I.H., Extramural

MeSH terms

  • ATP-Binding Cassette Transporters / chemistry
  • ATP-Binding Cassette Transporters / metabolism*
  • Binding Sites
  • Glutathione / chemistry*
  • Glutathione / metabolism
  • Iron / chemistry*
  • Iron / metabolism
  • Iron-Sulfur Proteins / chemistry
  • Iron-Sulfur Proteins / metabolism
  • Molecular Dynamics Simulation
  • Protein Structure, Tertiary
  • Static Electricity
  • Substrate Specificity
  • Sulfur / chemistry*
  • Sulfur / metabolism

Substances

  • ABCB7 protein, human
  • ATP-Binding Cassette Transporters
  • Iron-Sulfur Proteins
  • Sulfur
  • Iron
  • Glutathione