5UCX

Structure of S78C Human Peroxiredoxin 3 as three stacked rings

5UCX の概要

• エントリーDOI: 10.2210/pdb5ucx/pdb
• 関連するPDBエントリー: 1ZYE
• 分子名称: Thioredoxin-dependent peroxide reductase, mitochondrial (2 entities in total)
• 機能のキーワード: chaperone, stacked ring, peroxiredoxin 3, typical 2-cys, peroxidase, 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: 199892.04

構造登録者

Yewdall, N.A.,Gerrard, J.A.,Goldstone, G.C. (登録日: 2016-12-22, 公開日: 2018-01-10, 最終更新日: 2024-03-06)

主引用文献

Yewdall, N.A.,Peskin, A.V.,Hampton, M.B.,Goldstone, D.C.,Pearce, F.G.,Gerrard, J.A.
Quaternary structure influences the peroxidase activity of peroxiredoxin 3.
Biochem. Biophys. Res. Commun., 497:558-563, 2018

PubMed Abstract: Peroxiredoxins are abundant peroxidase enzymes that are key regulators of the cellular redox environment. A major subgroup of these proteins, the typical 2-Cys peroxiredoxins, can switch between dimers and decameric or dodecameric rings, during the catalytic cycle. The necessity of this change in quaternary structure for function as a peroxidase is not fully understood. In order to explore this, human peroxiredoxin 3 (Prx3) protein was engineered to form both obligate dimers (S75E Prx3) and stabilised dodecameric rings (S78C Prx3), uncoupling structural transformations from the catalytic cycle. The obligate dimer, S75E Prx3, retained catalytic activity towards hydrogen peroxide, albeit significantly lower than the wildtype and S78C proteins, suggesting an evolutionary advantage of having higher order self-assemblies.

PubMed: 29438714
DOI: 10.1016/j.bbrc.2018.02.093

実験手法

X-RAY DIFFRACTION (2.4 Å)