6G61
Crystal structure of thioredoxin O1 from Arabidopsis thaliana in oxidized state
Summary for 6G61
| Entry DOI | 10.2210/pdb6g61/pdb |
| Descriptor | Thioredoxin O1, mitochondrial (2 entities in total) |
| Functional Keywords | thioredoxin, oxidoreductase |
| Biological source | Arabidopsis thaliana (Mouse-ear cress) |
| Total number of polymer chains | 1 |
| Total formula weight | 14594.64 |
| Authors | Roret, T.,Didierjean, C. (deposition date: 2018-03-31, release date: 2018-10-24, Last modification date: 2024-10-16) |
| Primary citation | Zannini, F.,Roret, T.,Przybyla-Toscano, J.,Dhalleine, T.,Rouhier, N.,Couturier, J. MitochondrialArabidopsis thalianaTRXo Isoforms Bind an Iron−Sulfur Cluster and Reduce NFU Proteins In Vitro. Antioxidants (Basel), 7:-, 2018 Cited by PubMed Abstract: In plants, the mitochondrial thioredoxin (TRX) system generally comprises only one or two isoforms belonging to the TRX h or o classes, being less well developed compared to the numerous isoforms found in chloroplasts. Unlike most other plant species, possesses two TRXo isoforms whose physiological functions remain unclear. Here, we performed a structure⁻function analysis to unravel the respective properties of the duplicated TRXo1 and TRXo2 isoforms. Surprisingly, when expressed in , both recombinant proteins existed in an apo-monomeric form and in a homodimeric iron⁻sulfur (Fe-S) cluster-bridged form. In TRXo2, the [4Fe-4S] cluster is likely ligated in by the usual catalytic cysteines present in the conserved Trp-Cys-Gly-Pro-Cys signature. Solving the three-dimensional structure of both TRXo apo-forms pointed to marked differences in the surface charge distribution, notably in some area usually participating to protein⁻protein interactions with partners. However, we could not detect a difference in their capacity to reduce nitrogen-fixation-subunit-U (NFU)-like proteins, NFU4 or NFU5, two proteins participating in the maturation of certain mitochondrial Fe-S proteins and previously isolated as putative TRXo1 partners. Altogether, these results suggest that a novel regulation mechanism may prevail for mitochondrial TRXs o, possibly existing as a redox-inactive Fe-S cluster-bound form that could be rapidly converted in a redox-active form upon cluster degradation in specific physiological conditions. PubMed: 30322144DOI: 10.3390/antiox7100142 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.8 Å) |
Structure validation
Download full validation report
