title: A structural model for glutathione-complexed iron-sulfur cluster as a substrate for ABCB7-type transporters.
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.
authors.affiliation: Ohio State Biochemistry Program, The Ohio State University, USA. cowan@chemistry.ohio-state.edu.
authors.forename: Wenbin
authors.initials: W
authors.lastname: Qi
authors.forename: Jingwei
authors.initials: J
authors.lastname: Li
authors.forename: J A
authors.initials: JA
authors.lastname: Cowan
mesh_terms: D018528:ATP-Binding Cassette Transporters / Q000737:chemistry / Q000378:metabolism*; D001665:Binding Sites; D005978:Glutathione / Q000737:chemistry* / Q000378:metabolism; D007501:Iron / Q000737:chemistry* / Q000378:metabolism; D007506:Iron-Sulfur Proteins / Q000737:chemistry / Q000378:metabolism; D056004:Molecular Dynamics Simulation; D017434:Protein Structure, Tertiary; D055672:Static Electricity; D013379:Substrate Specificity; D013455:Sulfur / Q000737:chemistry* / Q000378:metabolism
chemical_list: C113037:ABCB7 protein, human; D018528:ATP-Binding Cassette Transporters; D007506:Iron-Sulfur Proteins; D013455:Sulfur; D007501:Iron; D005978:Glutathione