2RUF
Solution structure of the a' domain of thermophilic fungal protein disulfide (reduced form, 303K)
Summary for 2RUF
| Entry DOI | 10.2210/pdb2ruf/pdb |
| Related | 2kp1 2kp2 |
| NMR Information | BMRB: 11562 |
| Descriptor | Protein disulfide-isomerase (1 entity in total) |
| Functional Keywords | thioredoxin fold, isomerase, disulfide bond, endoplasmic reticulum, redox-active center |
| Biological source | Humicola insolens (Soft-rot fungus) |
| Cellular location | Endoplasmic reticulum lumen : P55059 |
| Total number of polymer chains | 1 |
| Total formula weight | 13123.91 |
| Authors | Inagaki, K.,Satoh, T.,Kato, K. (deposition date: 2014-03-31, release date: 2015-05-20, Last modification date: 2024-05-15) |
| Primary citation | Inagaki, K.,Satoh, T.,Yagi-Utsumi, M.,Le Gulluche, A.C.,Anzai, T.,Uekusa, Y.,Kamiya, Y.,Kato, K. Redox-coupled structural changes of the catalytic a' domain of protein disulfide isomerase. Febs Lett., 589:2690-2694, 2015 Cited by PubMed Abstract: Protein disulfide isomerase functions as a folding catalyst in the endoplasmic reticulum. Its b' and a' domains provide substrate-binding sites and undergo a redox-dependent domain rearrangement coupled to an open-closed structural change. Here we determined the first solution structure of the a' domain in its oxidized form and thereby demonstrate that oxidation of the a' domain induces significant conformational changes not only in the vicinity of the active site but also in the distal b'-interfacial segment. Based on these findings, we propose that this conformational transition triggers the domain segregation coupled with the exposure of the hydrophobic surface. PubMed: 26272828DOI: 10.1016/j.febslet.2015.07.041 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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