1W89
Structure of the reduced form of human thioredoxin 2
1W89 の概要
エントリーDOI | 10.2210/pdb1w89/pdb |
関連するPDBエントリー | 1UVZ 1W4V |
分子名称 | THIOREDOXIN (2 entities in total) |
機能のキーワード | antioxidant enzyme, mitochondrion, electron transport |
由来する生物種 | HOMO SAPIENS (HUMAN) |
タンパク質・核酸の鎖数 | 6 |
化学式量合計 | 79728.92 |
構造登録者 | |
主引用文献 | Smeets, A.,Evrard, C.,Landtmeters, M.,Marchand, C.,Knoops, B.,Declercq, J.P. Crystal Structures of Oxidized and Reduced Forms of Human Mitochondrial Thioredoxin 2. Protein Sci., 14:2610-, 2005 Cited by PubMed Abstract: Mammalian thioredoxin 2 is a mitochondrial isoform of highly evolutionary conserved thioredoxins. Thioredoxins are small ubiquitous protein-disulfide oxidoreductases implicated in a large variety of biological functions. In mammals, thioredoxin 2 is encoded by a nuclear gene and is targeted to mitochondria by a N-terminal mitochondrial presequence. Recently, mitochondrial thioredoxin 2 was shown to interact with components of the mitochondrial respiratory chain and to play a role in the control of mitochondrial membrane potential, regulating mitochondrial apoptosis signaling pathway. Here we report the first crystal structures of a mammalian mitochondrial thioredoxin 2. Crystal forms of reduced and oxidized human thioredoxin 2 are described at 2.0 and 1.8 A resolution. Though the folding is rather similar to that of human cytosolic/nuclear thioredoxin 1, important differences are observed during the transition between the oxidized and the reduced states of human thioredoxin 2, compared with human thioredoxin 1. In spite of the absence of the Cys residue implicated in dimer formation in human thioredoxin 1, dimerization still occurs in the crystal structure of human thioredoxin 2, mainly mediated by hydrophobic contacts, and the dimers are associated to form two-dimensional polymers. Interestingly, the structure of human thioredoxin 2 reveals possible interaction domains with human peroxiredoxin 5, a substrate protein of human thioredoxin 2 in mitochondria. PubMed: 16195549DOI: 10.1110/PS.051632905 主引用文献が同じPDBエントリー |
実験手法 | X-RAY DIFFRACTION (2 Å) |
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