3IPM

Crystal Structure of Archaeal 20S Proteasome in Complex with the C-terminus of PAN

3IPM の概要

• エントリーDOI: 10.2210/pdb3ipm/pdb
• EMDBエントリー: 5130
• 分子名称: Proteasome subunit alpha, Proteasome subunit beta, Proteasome activator PA26, Proteasome-activating nucleotidase fusion protein (3 entities in total)
• 機能のキーワード: proteasome, proteasomal atpase, protein degradation, aaa atpase, electron cryomicroscopy, hydrolase, protease, threonine protease, hydrolase-hydrolase activator complex, hydrolase/hydrolase activator
• 由来する生物種: Thermoplasma acidophilum; 詳細
• 細胞内の位置: Cytoplasm : P25156 P28061 Q58576
• タンパク質・核酸の鎖数: 21
• 化学式量合計: 533092.91

構造登録者

Yu, Y.,Cheng, Y. (登録日: 2009-08-17, 公開日: 2009-12-29, 最終更新日: 2023-09-06)

主引用文献

Yu, Y.,Smith, D.M.,Kim, H.M.,Rodriguez, V.,Goldberg, A.L.,Cheng, Y.
Interactions of PAN's C-termini with archaeal 20S proteasome and implications for the eukaryotic proteasome-ATPase interactions.
Embo J., 29:692-702, 2010

PubMed Abstract: Protein degradation in the 20S proteasome is regulated in eukaryotes by the 19S ATPase complex and in archaea by the homologous PAN ATPase ring complex. Subunits of these hexameric ATPases contain on their C-termini a conserved hydrophobic-tyrosine-X (HbYX) motif that docks into pockets in the 20S to stimulate the opening of a gated substrate entry channel. Here, we report the crystal structure of the archaeal 20S proteasome in complex with the C-terminus of the archaeal proteasome regulatory ATPase, PAN. This structure defines the detailed interactions between the critical C-terminal HbYX motif and the 20S alpha-subunits and indicates that the intersubunit pocket in the 20S undergoes an induced-fit conformational change on binding of the HbYX motif. This structure together with related mutagenesis data suggest how in eukaryotes certain proteasomal ATPases bind to specific pockets in an asymmetrical manner to regulate gate opening.

PubMed: 20019667
DOI: 10.1038/emboj.2009.382

実験手法

X-RAY DIFFRACTION (4 Å)