8RVO
Proteasomal late precursor complex from pre1-1, state 1
Summary for 8RVO
| Entry DOI | 10.2210/pdb8rvo/pdb |
| EMDB information | 19523 19527 19528 19529 51221 |
| Descriptor | Proteasome subunit beta type-6, Proteasome subunit alpha type-5, Proteasome subunit alpha type-6, ... (18 entities in total) |
| Functional Keywords | proteasome biogenesis, ump1, pre1-1, cryo-em, propertied maturation, hydrolase |
| Biological source | Saccharomyces cerevisiae (brewer's yeast) More |
| Total number of polymer chains | 34 |
| Total formula weight | 927155.63 |
| Authors | Mark, E.,Ramos, P.C.,Kayser, F.,Hoeckendorff, J.,Dohmen, R.J.,Wendler, P. (deposition date: 2024-02-01, release date: 2024-09-11, Last modification date: 2024-09-25) |
| Primary citation | Mark, E.,Ramos, P.C.,Kayser, F.,Hockendorff, J.,Dohmen, R.J.,Wendler, P. Structural roles of Ump1 and beta-subunit propeptides in proteasome biogenesis. Life Sci Alliance, 7:-, 2024 Cited by PubMed Abstract: The yeast (β4-S142F) mutant accumulates late 20S proteasome core particle precursor complexes (late-PCs). We report a 2.1 Å cryo-EM structure of this intermediate with full-length Ump1 trapped inside, and Pba1-Pba2 attached to the α-ring surfaces. The structure discloses intimate interactions of Ump1 with β2- and β5-propeptides, which together fill most of the antechambers between the α- and β-rings. The β5-propeptide is unprocessed and separates Ump1 from β6 and β7. The β2-propeptide is disconnected from the subunit by autocatalytic processing and localizes between Ump1 and β3. A comparison of different proteasome maturation states reveals that maturation goes along with global conformational changes in the rings, initiated by structuring of the proteolytic sites and their autocatalytic activation. In the strain, β2 is activated first enabling processing of β1-, β6-, and β7-propeptides. Subsequent maturation of β5 and β1 precedes degradation of Ump1, tightening of the complex, and finally release of Pba1-Pba2. PubMed: 39260885DOI: 10.26508/lsa.202402865 PDB entries with the same primary citation |
| Experimental method | ELECTRON MICROSCOPY (2.69 Å) |
Structure validation
Download full validation report
