5JCG

Structure of Human Peroxiredoxin 3 as three stacked rings

5JCG の概要

• エントリーDOI: 10.2210/pdb5jcg/pdb
• 分子名称: Thioredoxin-dependent peroxide reductase, mitochondrial (2 entities in total)
• 機能のキーワード: peroxidase, molecular chaperone, peroxiredoxin, oxidoreductase
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Mitochondrion: P30048
• タンパク質・核酸の鎖数: 9
• 化学式量合計: 199747.46

構造登録者

Yewdall, N.A.,Gerrard, J.A.,Goldstone, D.C. (登録日: 2016-04-15, 公開日: 2016-05-25, 最終更新日: 2023-09-27)

主引用文献

Yewdall, N.A.,Venugopal, H.,Desfosses, A.,Abrishami, V.,Yosaatmadja, Y.,Hampton, M.B.,Gerrard, J.A.,Goldstone, D.C.,Mitra, A.K.,Radjainia, M.
Structures of Human Peroxiredoxin 3 Suggest Self-Chaperoning Assembly that Maintains Catalytic State.
Structure, 24:1120-1129, 2016

PubMed Abstract: Peroxiredoxins are antioxidant proteins primarily responsible for detoxification of hydroperoxides in cells. On exposure to various cellular stresses, peroxiredoxins can acquire chaperone activity, manifested as quaternary reorganization into a high molecular weight (HMW) form. Acidification, for example, causes dodecameric rings of human peroxiredoxin 3 (HsPrx3) to stack into long helical filaments. In this work, a 4.1-Å resolution structure of low-pH-instigated helical filaments was elucidated, showing a locally unfolded active site and partially folded C terminus. A 2.8-Å crystal structure of HsPrx3 was determined at pH 8.5 under reducing conditions, wherein dodecameric rings are arranged as a short stack, with symmetry similar to low-pH filaments. In contrast to previous observations, the crystal structure displays both a fully folded active site and ordered C terminus, suggesting that the HsPrx3 HMW form maintains catalytic activity. We propose a new role for the HMW form as a self-chaperoning assembly maintaining HsPrx3 function under stress.

PubMed: 27238969
DOI: 10.1016/j.str.2016.04.013

実験手法

X-RAY DIFFRACTION (2.8 Å)