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