2QD0

Crystal structure of mitoNEET

2QD0 の概要

• エントリーDOI: 10.2210/pdb2qd0/pdb
• 分子名称: Zinc finger CDGSH domain-containing protein 1, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: iron-sulfur cluster, [2fe-2s], histidine ligation, metal binding protein
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 19111.22

構造登録者

Lin, J.,Zhou, T.,Ye, K.,Wang, J. (登録日: 2007-06-20, 公開日: 2007-08-28, 最終更新日: 2024-02-21)

主引用文献

Lin, J.,Zhou, T.,Ye, K.,Wang, J.
Crystal structure of human mitoNEET reveals distinct groups of iron sulfur proteins.
Proc.Natl.Acad.Sci.Usa, 104:14640-14645, 2007

PubMed Abstract: 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.

PubMed: 17766439
DOI: 10.1073/pnas.0702426104

実験手法

X-RAY DIFFRACTION (1.81 Å)