3O55

Crystal structure of human FAD-linked augmenter of liver regeneration (ALR)

3O55 の概要

• エントリーDOI: 10.2210/pdb3o55/pdb
• 関連するPDBエントリー: 2HJ3 3MBG
• 分子名称: Augmenter of liver regeneration, FLAVIN-ADENINE DINUCLEOTIDE (3 entities in total)
• 機能のキーワード: flavin, flavoprotein, sulfhydryl oxidase, fad, gfer, alr
• 由来する生物種: Homo sapiens (human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 15777.34

構造登録者

Banci, L.,Bertini, I.,Calderone, V.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A.,Kallergi, E.,Lionaki, E.,Pozidis, C.,Tokatlidis, K. (登録日: 2010-07-28, 公開日: 2011-04-13, 最終更新日: 2024-11-20)

主引用文献

Banci, L.,Bertini, I.,Calderone, V.,Cefaro, C.,Ciofi-Baffoni, S.,Gallo, A.,Kallergi, E.,Lionaki, E.,Pozidis, C.,Tokatlidis, K.
Molecular recognition and substrate mimicry drive the electron-transfer process between MIA40 and ALR.
Proc.Natl.Acad.Sci.USA, 108:4811-4816, 2011

PubMed Abstract: Oxidative protein folding in the mitochondrial intermembrane space requires the transfer of a disulfide bond from MIA40 to the substrate. During this process MIA40 is reduced and regenerated to a functional state through the interaction with the flavin-dependent sulfhydryl oxidase ALR. Here we present the mechanistic basis of ALR-MIA40 interaction at atomic resolution by biochemical and structural analyses of the mitochondrial ALR isoform and its covalent mixed disulfide intermediate with MIA40. This ALR isoform contains a folded FAD-binding domain at the C-terminus and an unstructured, flexible N-terminal domain, weakly and transiently interacting one with the other. A specific region of the N-terminal domain guides the interaction with the MIA40 substrate binding cleft (mimicking the interaction of the substrate itself), without being involved in the import of ALR. The hydrophobicity-driven binding of this region ensures precise protein-protein recognition needed for an efficient electron transfer process.

PubMed: 21383138
DOI: 10.1073/pnas.1014542108

実験手法

X-RAY DIFFRACTION (1.9 Å)