2qd0
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Crystal structure of mitoNEET
OverviewOverview
MitoNEET is a protein of unknown function present in the mitochondrial, membrane that was recently shown to bind specifically the antidiabetic, drug pioglizatone. Here, we report the crystal structure of the soluble, domain (residues 32-108) of human mitoNEET at 1.8-A resolution. The, structure reveals an intertwined homodimer, and each subunit was observed, to bind a [2Fe-2S] cluster. The [2Fe-2S] ligation pattern of three, cysteines and one histidine differs from the known pattern of four, cysteines in most cases or two cysteines and two histidines as observed in, Rieske proteins. The [2Fe-2S] cluster is packed in a modular structure, formed by 17 consecutive residues. The cluster-binding motif is conserved, in at least seven distinct groups of proteins from bacteria, archaea, and, eukaryotes, which show a consensus sequence of, (hb)-C-X(1)-C-X(2)-(S/T)-X(3)-P-(hb)-C-D-X(2)-H, where hb represents a, hydrophobic residue; we term this a CCCH-type [2Fe-2S] binding motif. The, nine conserved residues in the motif contribute to iron ligation and, structure stabilization. UV-visible absorption spectra indicated that, mitoNEET can exist in oxidized and reduced states. Our study suggests an, electron transfer function for mitoNEET and for other proteins containing, the CCCH motif.
About this StructureAbout this Structure
2QD0 is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.
ReferenceReference
Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins., Lin J, Zhou T, Ye K, Wang J, Proc Natl Acad Sci U S A. 2007 Sep 11;104(37):14640-5. Epub 2007 Aug 31. PMID:17766439 [[Category: [2fe-2s]]]
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