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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 ?M). 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.

SUBMITTER: Qi W

PROVIDER: S-EPMC4052440 | biostudies-literature | 2014 Apr

REPOSITORIES: biostudies-literature

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

Qi Wenbin W Li Jingwei J Cowan J A JA

Chemical communications (Cambridge, England) 20140401 29

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. ...[more]

PMID: 24584132

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