2R2J
crystal structure of human ERp44
Summary for 2R2J
| Entry DOI | 10.2210/pdb2r2j/pdb |
| Descriptor | Thioredoxin domain-containing protein 4, SUCCINIC ACID, FORMIC ACID, ... (4 entities in total) |
| Functional Keywords | thioredoxin, crfs motif, chaperone, endoplasmic reticulum, stress response |
| Biological source | Homo sapiens (Human) |
| Cellular location | Endoplasmic reticulum lumen: Q9BS26 |
| Total number of polymer chains | 1 |
| Total formula weight | 44770.87 |
| Authors | Wang, L.K.,Li, S.J.,Sun, F.,Wang, C.C. (deposition date: 2007-08-25, release date: 2008-07-08, Last modification date: 2011-07-13) |
| Primary citation | Wang, L.K.,Wang, L.,Vavassori, S.,Li, S.J.,Ke, H.,Anelli, T.,Degano, M.,Ronzoni, R.,Sitia, R.,Sun, F.,Wang, C.C. Crystal structure of human ERp44 shows a dynamic functional modulation by its carboxy-terminal tail. Embo Rep., 2008 Cited by PubMed Abstract: ERp44 mediates thiol-dependent retention in the early secretory pathway, forming mixed disulphides with substrate proteins through its conserved CRFS motif. Here, we present its crystal structure at a resolution of 2.6 A. Three thioredoxin domains-a, b and b'-are arranged in a clover-like structure. A flexible carboxy-terminal tail turns back to the b' and a domains, shielding a hydrophobic pocket in domain b' and a hydrophobic patch around the CRFS motif in domain a. Mutational and functional studies indicate that the C-terminal tail gates the CRFS area and the adjacent hydrophobic pocket, dynamically regulating protein quality control. PubMed: 18552768DOI: 10.1038/embor.2008.88 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2.6 Å) |
Structure validation
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