2R13

Crystal structure of human mitoNEET reveals a novel [2Fe-2S] cluster coordination

2R13 の概要

• エントリーDOI: 10.2210/pdb2r13/pdb
• 分子名称: Zinc finger CDGSH domain-containing protein 1, CHLORIDE ION, FE2/S2 (INORGANIC) CLUSTER, ... (4 entities in total)
• 機能のキーワード: beta-beta-alpha-beta topology, acetylation, metal-binding, zinc, zinc-finger, metal binding protein
• 由来する生物種: Homo sapiens (human)
• 細胞内の位置: Mitochondrion outer membrane ; Single- pass type III membrane protein : Q9NZ45
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 9431.86

構造登録者

Hou, X.,Liu, R.,Ross, S.,Smart, E.J.,Zhu, H.,Gong, W. (登録日: 2007-08-22, 公開日: 2007-09-11, 最終更新日: 2024-03-13)

主引用文献

Hou, X.,Liu, R.,Ross, S.,Smart, E.J.,Zhu, H.,Gong, W.
Crystallographic studies of human MitoNEET
J.Biol.Chem., 282:33242-33246, 2007

PubMed Abstract: MitoNEET was identified as an outer mitochondrial membrane protein that can potentially bind the anti-diabetes drug pioglitazone. The crystal structure of the cytoplasmic mitoNEET (residues 33-108) is determined in this study. The structure presents a novel protein fold and contains a [2Fe-2S] cluster-binding domain. The [2Fe-2S] cluster is coordinated to the protein by Cys-72, Cys-74, Cys-83, and His-87 residues. This coordination is also novel compared with the traditional [2Fe-2S] cluster coordinated by four cysteines or two cysteines and two histidines. The cytoplasmic mitoNEET forms homodimers in solution and in crystal. The dimerization is mainly mediated by hydrophobic interactions as well as hydrogen bonds coordinated by two water molecules binding at the interface. His-87 residue, which plays an important role in the coordination of the [2Fe-2S] cluster, is exposed to the solvent on the dimer surface. It is proposed that mitoNEET dimer may interact with other proteins via the surface residues in close proximity to the [2Fe-2S] cluster.

PubMed: 17905743
DOI: 10.1074/jbc.C700172200

実験手法

X-RAY DIFFRACTION (1.8 Å)