7V5G
20S+monoUb-CyclinB1-NT (S1)
Summary for 7V5G
| Entry DOI | 10.2210/pdb7v5g/pdb |
| EMDB information | 31724 |
| Descriptor | Proteasome subunit beta type-6, Proteasome subunit alpha type-4, Proteasome subunit alpha type-7, ... (14 entities in total) |
| Functional Keywords | 20s proteasome, human, substrate, ubiquitin, hydrolase |
| Biological source | Homo sapiens (Human) More |
| Total number of polymer chains | 28 |
| Total formula weight | 717751.33 |
| Authors | |
| Primary citation | Sahu, I.,Mali, S.M.,Sulkshane, P.,Xu, C.,Rozenberg, A.,Morag, R.,Sahoo, M.P.,Singh, S.K.,Ding, Z.,Wang, Y.,Day, S.,Cong, Y.,Kleifeld, O.,Brik, A.,Glickman, M.H. The 20S as a stand-alone proteasome in cells can degrade the ubiquitin tag. Nat Commun, 12:6173-6173, 2021 Cited by PubMed Abstract: The proteasome, the primary protease for ubiquitin-dependent proteolysis in eukaryotes, is usually found as a mixture of 30S, 26S, and 20S complexes. These complexes have common catalytic sites, which makes it challenging to determine their distinctive roles in intracellular proteolysis. Here, we chemically synthesize a panel of homogenous ubiquitinated proteins, and use them to compare 20S and 26S proteasomes with respect to substrate selection and peptide-product generation. We show that 20S proteasomes can degrade the ubiquitin tag along with the conjugated substrate. Ubiquitin remnants on branched peptide products identified by LC-MS/MS, and flexibility in the 20S gate observed by cryo-EM, reflect the ability of the 20S proteasome to proteolyze an isopeptide-linked ubiquitin-conjugate. Peptidomics identifies proteasome-trapped ubiquitin-derived peptides and peptides of potential 20S substrates in Hi20S cells, hypoxic cells, and human failing-heart. Moreover, elevated levels of 20S proteasomes appear to contribute to cell survival under stress associated with damaged proteins. PubMed: 34702852DOI: 10.1038/s41467-021-26427-0 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (4.47 Å) |
Structure validation
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