Summary for 4V7O
| Entry DOI | 10.2210/pdb4v7o/pdb |
| Related | 1Z7Q |
| Descriptor | Proteasome component C7-alpha, Proteasome component PUP3, Proteasome component C11, ... (17 entities in total) |
| Functional Keywords | 20s proteasome blm10, hydrolase, nucleus, phosphoprotein, protease, proteasome, threonine protease, isopeptide bond, zymogen |
| Biological source | Saccharomyces cerevisiae More |
| Cellular location | Cytoplasm : P21243 P25451 P22141 P30656 P23724 P30657 P23639 P23638 P40303 P32379 P40302 P21242 P38624 P25043 Nucleus: P43583 P43583 P43583 |
| Total number of polymer chains | 68 |
| Total formula weight | 2258055.15 |
| Authors | Hill, C.P.,Whitby, F.G. (deposition date: 2009-12-22, release date: 2014-07-09, Last modification date: 2024-04-03) |
| Primary citation | Sadre-Bazzaz, K.,Whitby, F.G.,Robinson, H.,Formosa, T.,Hill, C.P. Structure of a Blm10 complex reveals common mechanisms for proteasome binding and gate opening. Mol.Cell, 37:728-735, 2010 Cited by PubMed Abstract: The proteasome is an abundant protease that is critically important for numerous cellular pathways. Proteasomes are activated in vitro by three known classes of proteins/complexes, including Blm10/PA200. Here, we report a 3.4 A resolution crystal structure of a proteasome-Blm10 complex, which reveals that Blm10 surrounds the proteasome entry pore in the 1.2 MDa complex to form a largely closed dome that is expected to restrict access of potential substrates. This architecture and the observation that Blm10 induces a disordered proteasome gate structure challenge the assumption that Blm10 functions as an activator of proteolysis in vivo. The Blm10 C terminus binds in the same manner as seen for 11S activators and inferred for 19S/PAN activators and indicates a unified model for gate opening. We also demonstrate that Blm10 acts to maintain mitochondrial function. Consistent with the structural data, the C-terminal residues of Blm10 are needed for this activity. PubMed: 20227375DOI: 10.1016/j.molcel.2010.02.002 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.005 Å) |
Structure validation
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