3WHL

Crystal structure of Nas2 N-terminal domain complexed with PAN-Rpt5C chimera

3WHL の概要

• エントリーDOI: 10.2210/pdb3whl/pdb
• 関連するPDBエントリー: 2DZN 3ACP 3H4M 3VLD 3VLE 3VLF 3WHJ 3WHK
• 分子名称: Proteasome-activating nucleotidase, 26S protease regulatory subunit 6A, Probable 26S proteasome regulatory subunit p27, ADENOSINE-5'-TRIPHOSPHATE (3 entities in total)
• 機能のキーワード: four-helix bundle, proteasome atpase subunit, proteasome assembly chaperone, atp binding, hydrolase-chaperone complex, hydrolase/chaperone
• 由来する生物種: Pyrococcus furiosus (yeast); 詳細
• 細胞内の位置: Cytoplasm : P33297
• タンパク質・核酸の鎖数: 8
• 化学式量合計: 177568.70

構造登録者

Satoh, T.,Saeki, Y.,Hiromoto, T.,Wang, Y.-H.,Uekusa, Y.,Yagi, H.,Yoshihara, H.,Yagi-Utsumi, M.,Mizushima, T.,Tanaka, K.,Kato, K. (登録日: 2013-08-26, 公開日: 2014-03-26, 最終更新日: 2023-11-08)

主引用文献

Satoh, T.,Saeki, Y.,Hiromoto, T.,Wang, Y.H.,Uekusa, Y.,Yagi, H.,Yoshihara, H.,Yagi-Utsumi, M.,Mizushima, T.,Tanaka, K.,Kato, K.
Structural basis for proteasome formation controlled by an assembly chaperone nas2.
Structure, 22:731-743, 2014

PubMed Abstract: Proteasome formation does not occur due to spontaneous self-organization but results from a highly ordered process assisted by several assembly chaperones. The assembly of the proteasome ATPase subunits is assisted by four client-specific chaperones, of which three have been structurally resolved. Here, we provide the structural basis for the working mechanisms of the last, hereto structurally uncharacterized assembly chaperone, Nas2. We revealed that Nas2 binds to the Rpt5 subunit in a bivalent mode: the N-terminal helical domain of Nas2 masks the Rpt1-interacting surface of Rpt5, whereas its C-terminal PDZ domain caps the C-terminal proteasome-activating motif. Thus, Nas2 operates as a proteasome activation blocker, offering a checkpoint during the formation of the 19S ATPase prior to its docking onto the proteolytic 20S core particle.

PubMed: 24685148
DOI: 10.1016/j.str.2014.02.014

実験手法

X-RAY DIFFRACTION (4 Å)