InterPro domain: IPR042216

CDGSH iron-sulfur domains (CISDs) are classified into seven major types and are widely distributed throughout the three domains of life [ 1 ]. This superfamily represents the C-terminal domain found in the human CISD protein mitoNEET, also designated CSD1, an iron-containing integral protein of the outer mitochondrial membrane (OMM). MitoNEET contains two domains: a beta-cap region and a cluster-binding domain, containing the CDGSH motif, that coordinates two acid-labile 2Fe-2S clusters (one bound to each protomer) [ 2 ]. The CDGSH iron-sulphur domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates [ 3 , 4 ]. The whole protein regulates oxidative capacity and might be involved in electron transfer.

1. Structure and molecular evolution of CDGSH iron-sulfur domains. PLoS ONE 6, e24790
2. MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone. Proc. Natl. Acad. Sci. U.S.A. 104, 14342-7
3. The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster. J. Biol. Chem. 282, 23745-9