3REE

Crystal structure of mitoNEET

3REE の概要

• エントリーDOI: 10.2210/pdb3ree/pdb
• 分子名称: CDGSH iron-sulfur domain-containing protein 1, FE2/S2 (INORGANIC) CLUSTER (3 entities in total)
• 機能のキーワード: mitoneet, fes cluster, fes, 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: 9951.13

構造登録者

Funk, M.O.,Arif, W.,Xu, S.,Mueser, T.C. (登録日: 2011-04-04, 公開日: 2011-04-13, 最終更新日: 2023-09-13)

主引用文献

Arif, W.,Xu, S.,Isailovic, D.,Geldenhuys, W.J.,Carroll, R.T.,Funk, M.O.
Complexes of the Outer Mitochondrial Membrane Protein MitoNEET with Resveratrol-3-Sulfate.
Biochemistry, 50:5806-5811, 2011

PubMed Abstract: Binding of the thiazolidinedione antidiabetic drug pioglitazone led to the discovery of a novel outer mitochondrial membrane protein of unknown function called mitoNEET. The protein is homodimeric and contains a uniquely ligated two iron-two sulfur cluster in each of its two cytosolic domains. Electrospray ionization mass spectrometry was employed to characterize solutions of the soluble cytosolic domain (amino acids 32--108) of the protein. Ions characteristic of dimers containing the cofactors were readily detected under native conditions. mitoNEET responded to exposure to solutions at low pH by dissociation to give monomers that retained the cofactor, followed by dissociation of the cofactor in a concerted fashion. mitoNEET formed complexes with resveratrol-3-sulfate, one of the primary metabolites of the natural product resveratrol. Resveratrol itself showed no tendency to interact with mitoNEET. The formation of complexes was evident in both electrospray ionization mass spectrometry and isothermal titration calorimetry measurements. Up to eight molecules of the compound associated with the dimeric form of the protein in a sequential fashion. Dissociation constants determined by micorcalorimetry were in the range 5-16 μM for the various binding sites. The only other known naturally occurring binding partner for mitoNEET at present is NADPH. It is very interesting that the iron-sulfur cluster containing protein interacts with two potentially redox active substances at the surface of mitochondria. These findings provide a new direction for research into two poorly understood, yet biomedically relevant, species.

PubMed: 21591687
DOI: 10.1021/bi200546s

実験手法

X-RAY DIFFRACTION (1.76 Å)