37EI
Solution structure of the Cys-rich domain of the 15 kDa selenoprotein
Summary for 37EI
| Entry DOI | 10.2210/pdb37ei/pdb |
| NMR Information | BMRB: 31309 |
| Descriptor | Selenoprotein F (1 entity in total) |
| Functional Keywords | endoplasmic reticulum, chaperone |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 11488.73 |
| Authors | |
| Primary citation | Williams, R.V.,Guay, K.P.,Lesk, O.H.,Hebert, D.N.,Gierasch, L.M. The cysteine-rich domain of SEP15, a selenoprotein co-chaperone of the ER chaperone, UDP-glucose:glycoprotein glucosyltransferase, adopts a novel fold. J.Biol.Chem., :113629-113629, 2026 Cited by PubMed Abstract: Proteins targeted to the secretory pathway are involved in a myriad of biological processes but can only do so when properly folded. Within the endoplasmic reticulum, glycoprotein folding is regulated by the enzyme UDP-glucose:glycoprotein glucosyltransferase (UGGT) and its oxidoreductase partner, the 15-kDa selenoprotein (SEP15 aka SELENOF). The interaction between these two chaperones is poorly understood, limiting understanding of their function. SEP15 is comprised of two domains, a C-terminal thioredoxin-like domain, the structure of which has been reported (PDB 2A4H), and an approximately 50-residue long N-terminal cysteine-rich domain (CRD), of unknown structure. Here, we report the NMR solution structure of SEP15 CRD, which mediates the interaction with UGGT. These data reveal that this domain adopts a dimer in solution and forms a previously undescribed helical fold, stabilized by three disulfide bonds between residues C10-C42, C21-C43, and C24-C39. Furthermore, our results validate a model of the UGGT/SEP15 complex and lay the foundation for future studies of its interaction with glycoprotein substrates. PubMed: 42854909DOI: 10.1016/j.jbc.2026.113629 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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