6UTI
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome with singly capped PAN complex
Summary for 6UTI
Entry DOI | 10.2210/pdb6uti/pdb |
EMDB information | 20877 20878 20879 20880 20881 |
Descriptor | Proteasome subunit alpha, Proteasome subunit beta (3 entities in total) |
Functional Keywords | pan, proteasome, singly-capped, hydrolase |
Biological source | Thermoplasma acidophilum More |
Total number of polymer chains | 28 |
Total formula weight | 663171.59 |
Authors | |
Primary citation | Yu, Z.,Yu, Y.,Wang, F.,Myasnikov, A.G.,Coffino, P.,Cheng, Y. Allosteric coupling between alpha-rings of the 20S proteasome. Nat Commun, 11:4580-4580, 2020 Cited by PubMed Abstract: Proteasomal machinery performs essential regulated protein degradation in eukaryotes. Classic proteasomes are symmetric, with a regulatory ATPase docked at each end of the cylindrical 20S. Asymmetric complexes are also present in cells, either with a single ATPase or with an ATPase and non-ATPase at two opposite ends. The mechanism that populates these different proteasomal complexes is unknown. Using archaea homologs, we construct asymmetric forms of proteasomes. We demonstrate that the gate conformation of the two opposite ends of 20S are coupled: binding one ATPase opens a gate locally, and also opens the opposite gate allosterically. Such allosteric coupling leads to cooperative binding of proteasomal ATPases to 20S and promotes formation of proteasomes symmetrically configured with two identical ATPases. It may also promote formation of asymmetric complexes with an ATPase and a non-ATPase at opposite ends. We propose that in eukaryotes a similar mechanism regulates the composition of the proteasomal population. PubMed: 32917864DOI: 10.1038/s41467-020-18415-7 PDB entries with the same primary citation |
Experimental method | ELECTRON MICROSCOPY (3.4 Å) |
Structure validation
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