3WXR
Yeast 20S proteasome with a mutation of alpha7 subunit
Summary for 3WXR
| Entry DOI | 10.2210/pdb3wxr/pdb |
| Descriptor | Proteasome subunit alpha type-1, Proteasome subunit beta type-3, Proteasome subunit beta type-4, ... (14 entities in total) |
| Functional Keywords | ups, 20s proteasome, hydrolase, protease, 19s regulatory particle, multicatalytic protease |
| Biological source | Saccharomyces cerevisiae S288c (yeast) More |
| Cellular location | Cytoplasm : P21243 P25451 P22141 P30656 P23724 P30657 P23639 P23638 P40303 P32379 P40302 P21242 P38624 P25043 |
| Total number of polymer chains | 28 |
| Total formula weight | 773413.01 |
| Authors | Yashiroda, H.,Toda, Y.,Otsu, S.,Takagi, K.,Mizushima, T.,Murata, S. (deposition date: 2014-08-06, release date: 2014-10-22, Last modification date: 2023-11-08) |
| Primary citation | Yashiroda, H.,Toda, Y.,Otsu, S.,Takagi, K.,Mizushima, T.,Murata, S. N-terminal alpha 7 deletion of the proteasome 20S core particle substitutes for yeast PI31 function Mol.Cell.Biol., 35:141-152, 2015 Cited by PubMed Abstract: The proteasome core particle (CP) is a conserved protease complex that is formed by the stacking of two outer α-rings and two inner β-rings. The α-ring is a heteroheptameric ring of subunits α1 to α7 and acts as a gate that restricts entry of substrate proteins into the catalytic cavity formed by the two abutting β-rings. The 31-kDa proteasome inhibitor (PI31) was originally identified as a protein that binds to the CP and inhibits CP activity in vitro, but accumulating evidence indicates that PI31 is required for physiological proteasome activity. To clarify the in vivo role of PI31, we examined the Saccharomyces cerevisiae PI31 ortholog Fub1. Fub1 was essential in a situation where the CP assembly chaperone Pba4 was deleted. The lethality of Δfub1 Δpba4 was suppressed by deletion of the N terminus of α7 (α7ΔN), which led to the partial activation of the CP. However, deletion of the N terminus of α3, which activates the CP more efficiently than α7ΔN by gate opening, did not suppress Δfub1 Δpba4 lethality. These results suggest that the α7 N terminus has a role in CP activation different from that of the α3 N terminus and that the role of Fub1 antagonizes a specific function of the α7 N terminus. PubMed: 25332237DOI: 10.1128/MCB.00582-14 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.15 Å) |
Structure validation
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