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TitleAllosteric coupling between α-rings of the 20S proteasome.
Journal, issue, pagesNat Commun, Vol. 11, Issue 1, Page 4580, Year 2020
Publish dateSep 11, 2020
AuthorsZanlin Yu / Yadong Yu / Feng Wang / Alexander G Myasnikov / Philip Coffino / Yifan Cheng /
PubMed AbstractProteasomal 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 ...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.
External linksNat Commun / PubMed:32917864 / PubMed Central
MethodsEM (single particle)
Resolution2.87 - 3.4 Å
Structure data

EMDB-20760:
PA26PANc-T20S singly-capped
Method: EM (single particle) / Resolution: 2.87 Å

20877

6utf

EMDB-20877, PDB-6utf:
Allosteric coupling between alpha-rings of the 20S proteasome, archaea 20S proteasome singly capped with a PAN complex
Method: EM (single particle) / Resolution: 3.4 Å

20878

6utg

EMDB-20878, PDB-6utg:
Allosteric coupling between alpha-rings of the 20S proteasome, 20S singly capped with a PA26/V230F
Method: EM (single particle) / Resolution: 3.4 Å

20879

6uth

EMDB-20879, PDB-6uth:
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome singly capped with a PA26/E102A_PANc, together with LFP incubation
Method: EM (single particle) / Resolution: 3.4 Å

20880

6uti

EMDB-20880, PDB-6uti:
Allosteric coupling between alpha-rings of 20S proteasome, 20S proteasome with singly capped PAN complex
Method: EM (single particle) / Resolution: 3.4 Å

20881

6utj

EMDB-20881: Allosteric couple between alpha rings of the 20S proteasome, 20S proteasome singly capped by PA26/E102A, C-terminus replaced by PAN C-terminus
PDB-6utj: Allosteric couple between alpha rings of the 20S proteasome. 20S proteasome singly capped by PA26/E102A, C-terminus replaced by PAN C-terminus
Method: EM (single particle) / Resolution: 2.9 Å

Source
  • thermoplasma acidophilum (acidophilic)
  • trypanosoma brucei (eukaryote)
  • trypanosoma brucei brucei (eukaryote)
KeywordsHYDROLASE / proteasome / PAN / singly-capped / PA26/V230F / PA26PANc / substrate LFP / PA26/E102A_PANc

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