2K3J

The solution structure of human Mia40

2K3J の概要

• エントリーDOI: 10.2210/pdb2k3j/pdb
• NMR情報: BMRB: 15763
• 分子名称: Mitochondrial intermembrane space import and assembly protein 40 (1 entity in total)
• 機能のキーワード: alpha-hairpin fold, coiled coil-helix-coiled coil-helix domain, mitochondrial oxidase, protein import and folding, alternative splicing, mitochondrion, protein transport, translocation, transport, oxidoreductase
• 由来する生物種: Homo sapiens
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16403.76

構造登録者

Ciofi Baffoni, S.,Bertini, I.,Gallo, A. (登録日: 2008-05-08, 公開日: 2009-02-10, 最終更新日: 2024-11-20)

主引用文献

Banci, L.,Bertini, I.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A.,Martinelli, M.,Sideris, D.P.,Katrakili, N.,Tokatlidis, K.
MIA40 is an oxidoreductase that catalyzes oxidative protein folding in mitochondria.
Nat.Struct.Mol.Biol., 16:198-206, 2009

PubMed Abstract: MIA40 has a key role in oxidative protein folding in the mitochondrial intermembrane space. We present the solution structure of human MIA40 and its mechanism as a catalyst of oxidative folding. MIA40 has a 66-residue folded domain made of an alpha-helical hairpin core stabilized by two structural disulfides and a rigid N-terminal lid, with a characteristic CPC motif that can donate its disulfide bond to substrates. The CPC active site is solvent-accessible and sits adjacent to a hydrophobic cleft. Its second cysteine (Cys55) is essential in vivo and is crucial for mixed disulfide formation with the substrate. The hydrophobic cleft functions as a substrate binding domain, and mutations of this domain are lethal in vivo and abrogate binding in vitro. MIA40 represents a thioredoxin-unrelated, minimal oxidoreductase, with a facile CPC redox active site that ensures its catalytic function in oxidative folding in mitochondria.

PubMed: 19182799
DOI: 10.1038/nsmb.1553

実験手法

SOLUTION NMR