2KR0
Solution structure of the proteasome ubiquitin receptor Rpn13
Summary for 2KR0
| Entry DOI | 10.2210/pdb2kr0/pdb |
| Related | 2KQZ 2R2Y 2Z4D 2Z59 3IHR |
| Descriptor | Proteasomal ubiquitin receptor ADRM1 (1 entity in total) |
| Functional Keywords | proteasome, ubiquitin, 19s regulator, protein binding |
| Biological source | Homo sapiens (human) |
| Cellular location | Cytoplasm : Q16186 |
| Total number of polymer chains | 1 |
| Total formula weight | 42485.38 |
| Authors | Chen, X.,Lee, B.,Finley, D.,Walters, K.J. (deposition date: 2009-11-25, release date: 2010-05-26, Last modification date: 2024-05-01) |
| Primary citation | Chen, X.,Lee, B.H.,Finley, D.,Walters, K.J. Structure of Proteasome Ubiquitin Receptor hRpn13 and Its Activation by the Scaffolding Protein hRpn2. Mol.Cell, 38:404-415, 2010 Cited by PubMed Abstract: Rpn13 is a subunit of the proteasome that serves as a receptor for both ubiquitin and Uch37, one of the proteasome's three deubiquitinating enzymes. We have determined the structure of full-length human Rpn13 (hRpn13). Unexpectedly, Rpn13's ubiquitin- and Uch37-binding domains pack against each other when it is not incorporated into the proteasome. This intramolecular interaction reduces hRpn13's affinity for ubiquitin. We find that hRpn13 binding to the proteasome scaffolding protein hRpn2/S1 abrogates its interdomain interactions, thus activating hRpn13 for ubiquitin binding. hRpn13's Uch37-binding domain, a previously unknown fold, contains nine alpha helices. We have mapped its Uch37-binding surface to a region rich in charged amino acids. Altogether, our results provide mechanistic insights into hRpn13's functional activities with Uch37 and ubiquitin and suggest that its role as a ubiquitin receptor is finely tuned for proteasome targeting. PubMed: 20471946DOI: 10.1016/j.molcel.2010.04.019 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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