5KQA
Crystal structure of buckwheat glutaredoxin-glutathione complex
Summary for 5KQA
| Entry DOI | 10.2210/pdb5kqa/pdb |
| Descriptor | Glutaredoxin-glutathione complex, GLUTATHIONE (3 entities in total) |
| Functional Keywords | glutaredoxin, glutathione, complex, monomer, oxidoreductase |
| Biological source | Polygonaceae (buckwheat family) |
| Total number of polymer chains | 1 |
| Total formula weight | 14454.41 |
| Authors | |
| Primary citation | Zhang, X.,Wang, W.,Li, C.,Zhao, Y.,Yuan, H.,Tan, X.,Wu, L.,Wang, Z.,Wang, H. Structural insights into the binding of buckwheat glutaredoxin with GSH and regulation of its catalytic activity J. Inorg. Biochem., 173:21-27, 2017 Cited by PubMed Abstract: Glutaredoxins (Grxs) are ubiquitous thioltransferases and members of the thioredoxin (Trx) fold superfamily. They have multiple functions in cells including oxidative stress responses and cell signaling. A novel glutaredoxin from buckwheat (rbGrx) with higher catalytic activity was identified, cloned, and purified. The structures of glutathionylated rbGrx and an rbGrx mutant, in which cysteine 39 was mutated to alanine, were solved by x-ray diffraction at a resolution of 2.05Å and 2.29Å, respectively. In rbGrx, GSH (glutathione) is bound at the conserved GSH-binding site, and its structure shows that it has the potential to function as a scaffold protein for the assembly and delivery of GSH. The crystal structure shows that GSH does not bind to the C39A rbGrx mutant, and the C39A mutant had no catalytic activity, indicating that C39 is a key residue that is involved in both the binding of rbGrx to GSH and the regulation of its catalytic activity. The model showing the binding of GSH with rbGrx provides a basis for understanding its molecular function and its potential future applications in medicinal food science. PubMed: 28478310DOI: 10.1016/j.jinorgbio.2017.04.019 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.05 Å) |
Structure validation
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