5JCG
Structure of Human Peroxiredoxin 3 as three stacked rings
Summary for 5JCG
| Entry DOI | 10.2210/pdb5jcg/pdb |
| Descriptor | Thioredoxin-dependent peroxide reductase, mitochondrial (2 entities in total) |
| Functional Keywords | peroxidase, molecular chaperone, peroxiredoxin, oxidoreductase |
| Biological source | Homo sapiens (Human) |
| Cellular location | Mitochondrion: P30048 |
| Total number of polymer chains | 9 |
| Total formula weight | 199747.46 |
| Authors | Yewdall, N.A.,Gerrard, J.A.,Goldstone, D.C. (deposition date: 2016-04-15, release date: 2016-05-25, Last modification date: 2023-09-27) |
| Primary citation | 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 Cited by 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: 27238969DOI: 10.1016/j.str.2016.04.013 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.8 Å) |
Structure validation
Download full validation report
