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-Structure paper
タイトル | Allosteric coupling between α-rings of the 20S proteasome. |
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ジャーナル・号・ページ | Nat Commun, Vol. 11, Issue 1, Page 4580, Year 2020 |
掲載日 | 2020年9月11日 |
著者 | Zanlin Yu / Yadong Yu / Feng Wang / Alexander G Myasnikov / Philip Coffino / Yifan Cheng / |
PubMed 要旨 | 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 ...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. |
リンク | Nat Commun / PubMed:32917864 / PubMed Central |
手法 | EM (単粒子) |
解像度 | 2.87 - 3.4 Å |
構造データ | EMDB-20760: EMDB-20877, PDB-6utf: EMDB-20878, PDB-6utg: EMDB-20879, PDB-6uth: EMDB-20880, PDB-6uti: 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 |
由来 |
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キーワード | HYDROLASE / proteasome / PAN / singly-capped / PA26/V230F / PA26PANc / substrate LFP / PA26/E102A_PANc |