8RVO

Proteasomal late precursor complex from pre1-1, state 1

8RVO の概要

• エントリーDOI: 10.2210/pdb8rvo/pdb
• EMDBエントリー: 19523 19527 19528 19529 51221
• 分子名称: Proteasome subunit beta type-6, Proteasome subunit alpha type-5, Proteasome subunit alpha type-6, ... (18 entities in total)
• 機能のキーワード: proteasome biogenesis, ump1, pre1-1, cryo-em, propertied maturation, hydrolase
• 由来する生物種: Saccharomyces cerevisiae (brewer's yeast); 詳細
• タンパク質・核酸の鎖数: 34
• 化学式量合計: 927155.63

構造登録者

Mark, E.,Ramos, P.C.,Kayser, F.,Hoeckendorff, J.,Dohmen, R.J.,Wendler, P. (登録日: 2024-02-01, 公開日: 2024-09-11, 最終更新日: 2024-09-25)

主引用文献

Mark, E.,Ramos, P.C.,Kayser, F.,Hockendorff, J.,Dohmen, R.J.,Wendler, P.
Structural roles of Ump1 and beta-subunit propeptides in proteasome biogenesis.
Life Sci Alliance, 7:-, 2024

PubMed Abstract: The yeast (β4-S142F) mutant accumulates late 20S proteasome core particle precursor complexes (late-PCs). We report a 2.1 Å cryo-EM structure of this intermediate with full-length Ump1 trapped inside, and Pba1-Pba2 attached to the α-ring surfaces. The structure discloses intimate interactions of Ump1 with β2- and β5-propeptides, which together fill most of the antechambers between the α- and β-rings. The β5-propeptide is unprocessed and separates Ump1 from β6 and β7. The β2-propeptide is disconnected from the subunit by autocatalytic processing and localizes between Ump1 and β3. A comparison of different proteasome maturation states reveals that maturation goes along with global conformational changes in the rings, initiated by structuring of the proteolytic sites and their autocatalytic activation. In the strain, β2 is activated first enabling processing of β1-, β6-, and β7-propeptides. Subsequent maturation of β5 and β1 precedes degradation of Ump1, tightening of the complex, and finally release of Pba1-Pba2.

PubMed: 39260885
DOI: 10.26508/lsa.202402865

実験手法

ELECTRON MICROSCOPY (2.69 Å)