Protein Family Models

The CDGSH-type zinc finger domain binds iron rather than zinc as a redox-active pH-labile 2Fe-2S cluster. The conserved sequence C-X-C-X2-(S/T)-X3-P-X-C-D-G-(S/A/T)-H is a defining feature of this family [1]. The domain is oriented towards the cytoplasm and is tethered to the mitochondrial membrane by a more N-terminal domain found in higher vertebrates, MitoNEET_N, Pfam:PF10660 [2]. The domain forms a uniquely folded homo-dimer and spans the outer mitochondrial membrane, orienting the iron-binding residues towards the cytoplasm [3]. [1]. 17376863. MitoNEET is an iron-containing outer mitochondrial membrane protein that regulates oxidative capacity. Wiley SE, Murphy AN, Ross SA, van der Geer P, Dixon JE;. Proc Natl Acad Sci U S A. 2007;104:5318-5323. [2]. 17584744. The outer mitochondrial membrane protein mitoNEET contains a novel redox-active 2Fe-2S cluster. Wiley SE, Paddock ML, Abresch EC, Gross L, van der Geer P, Nechushtai R, Murphy AN, Jennings PA, Dixon JE;. J Biol Chem. 2007;282:23745-23749. [3]. 17766440. MitoNEET is a uniquely folded 2Fe 2S outer mitochondrial membrane protein stabilized by pioglitazone. Paddock ML, Wiley SE, Axelrod HL, Cohen AE, Roy M, Abresch EC, Capraro D, Murphy AN, Nechushtai R, Dixon JE, Jennings PA;. Proc Natl Acad Sci U S A. 2007;104:14342-14347. (from Pfam)

Date:

2024-10-16

Members of this family contain three highly conserved cysteine residues. This family includes proteins containing divergent domains which are most likely to bind to iron-sulfur clusters. (from Pfam)

Date:

2024-08-14