3IPZ
Crystal structure of Arabidopsis monothiol glutaredoxin AtGRXcp
Summary for 3IPZ
| Entry DOI | 10.2210/pdb3ipz/pdb |
| Descriptor | Monothiol glutaredoxin-S14, chloroplastic (2 entities in total) |
| Functional Keywords | glutaredoxin, monothiol, chloroplast, electron transport, plastid, redox-active center, transit peptide, transport, oxidoreductase |
| Biological source | Arabidopsis thaliana (mouse-ear cress) |
| Cellular location | Plastid, chloroplast: Q84Y95 |
| Total number of polymer chains | 1 |
| Total formula weight | 12354.15 |
| Authors | |
| Primary citation | Li, L.,Cheng, N.,Hirschi, K.D.,Wang, X. Structure of Arabidopsis chloroplastic monothiol glutaredoxin AtGRXcp. Acta Crystallogr.,Sect.D, 66:725-732, 2010 Cited by PubMed Abstract: Monothiol glutaredoxins (Grxs) play important roles in maintaining redox homeostasis in living cells and are conserved across species. Arabidopsis thaliana monothiol glutaredoxin AtGRXcp is critical for protection from oxidative stress in chloroplasts. The crystal structure of AtGRXcp has been determined at 2.4 A resolution. AtGRXcp has a glutaredoxin/thioredoxin-like fold with distinct structural features that differ from those of dithiol Grxs. The structure reveals that the putative active-site motif CGFS is well defined and is located on the molecular surface and that a long groove extends to both sides of the catalytic Cys97. Structural comparison and molecular modeling suggest that glutathione can bind in this groove and form extensive interactions with conserved charged residues including Lys89, Arg126 and Asp152. Further comparative studies reveal that a unique loop with five additional residues adjacent to the active-site motif may be a key structural feature of monothiol Grxs and may influence their function. This study provides the first structural information on plant CGFS-type monothiol Grxs, allowing a better understanding of the redox-regulation mechanism mediated by these plant Grxs. PubMed: 20516625DOI: 10.1107/S0907444910013119 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.4 Å) |
Structure validation
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