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| Title | Atomic resolution Cryo-EM structure of human proteasome activator PA28γ. |
|---|---|
| Journal, issue, pages | Int J Biol Macromol, Vol. 219, Page 500-507, Year 2022 |
| Publish date | Aug 4, 2022 |
 Authors | Dan-Dan Chen / Jia Hao / Chao-Hui Shen / Xian-Ming Deng / Cai-Hong Yun /  |
| PubMed Abstract | The PA28 family proteasome activators play important roles in regulating proteasome activities. Though the three paralogs (PA28α, PA28β, and PA28γ) are similar in terms of primary sequence, they ...The PA28 family proteasome activators play important roles in regulating proteasome activities. Though the three paralogs (PA28α, PA28β, and PA28γ) are similar in terms of primary sequence, they show significant differences in expression pattern, cellular localization and most importantly, biological functions. While PA28αβ is responsible for promoting peptidase activity of proteasome to facilitate MHC-I antigen processing, but unable to promote protein degradation, PA28γ is well-known to not only promote peptidase activity but also proteolytic activity of proteasome. However, why this paralog has the unique function remains elusive. Previous structural studies have mainly focused on mammalian PA28α, PA28β and PA28αβ heptamers, while structural studies on mammalian PA28γ of atomic resolution are still absent to date. In the present work, we determined the Cryo-EM structure of the human PA28γ heptamer at atomic resolution, revealing interesting unique structural features that may hint our understanding the functional mechanisms of this proteasome activator. |
 External links | Int J Biol Macromol / PubMed:35932807 |
| Methods | EM (single particle) |
| Resolution | 2.82 - 3.4 Å |
| Structure data | EMDB-34023, PDB-7yqc: EMDB-34024, PDB-7yqd: |
| Source |
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 Keywords |  PROTEIN TRANSPORT / proteasome activator gamma / PA28gamma / PSME3 |
