2MWS
Structure of the complex of ubiquitin and the ubiquitin-like (UBL) domain of Ddi1
Summary for 2MWS
Entry DOI | 10.2210/pdb2mws/pdb |
NMR Information | BMRB: 25088 |
Descriptor | Ubiquitin, DNA damage-inducible protein 1 (2 entities in total) |
Functional Keywords | ubl, ddi1, ubiquitin, proteasome, protein transport |
Biological source | Homo sapiens (Human) More |
Cellular location | Ubiquitin: Cytoplasm : P0CG48 Cytoplasm : P40087 |
Total number of polymer chains | 2 |
Total formula weight | 19354.06 |
Authors | Fushman, D.,Nowicka, U.,Walker, O. (deposition date: 2014-11-23, release date: 2015-03-25, Last modification date: 2023-06-14) |
Primary citation | Nowicka, U.,Zhang, D.,Walker, O.,Krutauz, D.,Castaneda, C.A.,Chaturvedi, A.,Chen, T.Y.,Reis, N.,Glickman, M.H.,Fushman, D. DNA-Damage-Inducible 1 Protein (Ddi1) Contains an Uncharacteristic Ubiquitin-like Domain that Binds Ubiquitin. Structure, 23:542-557, 2015 Cited by PubMed Abstract: Ddi1 belongs to a family of shuttle proteins targeting polyubiquitinated substrates for proteasomal degradation. Unlike the other proteasomal shuttles, Rad23 and Dsk2, Ddi1 remains an enigma: its function is not fully understood and structural properties are poorly characterized. We determined the structure and binding properties of the ubiquitin-like (UBL) and ubiquitin-associated (UBA) domains of Ddi1 from Saccharomyces cerevisiae. We found that while Ddi1UBA forms a characteristic UBA:ubiquitin complex, Ddi1UBL has entirely uncharacteristic binding preferences. Despite having a ubiquitin-like fold, Ddi1UBL does not interact with typical UBL receptors but unexpectedly binds ubiquitin, forming a unique interface mediated by hydrophobic contacts and by salt bridges between oppositely charged residues of Ddi1UBL and ubiquitin. In stark contrast to ubiquitin and other UBLs, the β-sheet surface of Ddi1UBL is negatively charged and therefore is recognized in a completely different way. The dual functionality of Ddi1UBL, capable of binding both ubiquitin and proteasome, suggests an intriguing mechanism for Ddi1 as a proteasomal shuttle. PubMed: 25703377DOI: 10.1016/j.str.2015.01.010 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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