1J2Q

20S proteasome in complex with calpain-Inhibitor I from archaeoglobus fulgidus

1J2Q の概要

• エントリーDOI: 10.2210/pdb1j2q/pdb
• 関連するPDBエントリー: 1J2P
• 分子名称: Proteasome alpha subunit, Proteasome beta subunit, 2-ACETYLAMINO-4-METHYL-PENTANOIC ACID [1-(1-FORMYL-PENTYLCARBAMOYL)-3-METHYL-BUTYL]-AMIDE, ... (4 entities in total)
• 機能のキーワード: proteasome, ubiquitin, 20s, cp, hydrolase
• 由来する生物種: Archaeoglobus fulgidus; 詳細
• 細胞内の位置: Cytoplasm (By similarity): O29760 Q9P996
• タンパク質・核酸の鎖数: 14
• 化学式量合計: 343541.30

構造登録者

Groll, M.,Brandstetter, H.,Bartunik, H.,Bourenkow, G.,Huber, R. (登録日: 2003-01-08, 公開日: 2003-03-18, 最終更新日: 2024-12-25)

主引用文献

Groll, M.,Brandstetter, H.,Bartunik, H.,Bourenkow, G.,Huber, R.
Investigations on the Maturation and Regulation of Archaebacterial Proteasomes
J.MOL.BIOL., 327:75-83, 2003

PubMed Abstract: The 20S proteasome (core particle, CP) is a multifunctional protease complex and composed of four heptameric subunit rings arranged in a hollow, barrel-shaped structure. Here, we report the crystal structure of the CP from Archaeoglobus fulgidus at 2.25A resolution. The analysis of the structure of early and late assembly intermediates of this CP gives new insights in the maturation of archaebacterial CPs and indicates similarities to assembly intermediates observed in eukaryotes. We also show a striking difference in mechanism and regulation of substrate access between eukaryotic and archaebacterial 20S proteasomes. While eukaryotic CPs are auto-inhibited by the N-terminal tails of the outer alpha-ring by imposing topological closure with a characteristic sequence motif (YDR-motif) and show regulatory gating this segment is disordered in the CP and differently structured in the alpha(7)-sub-complex of A.fulgidus leaving a pore leading into the particle with a diameter of 13A. Mutagenesis and functional studies indicate the absence of regulatory gating in the archaeal 20S proteasome.

PubMed: 12614609
DOI: 10.1016/S0022-2836(03)00080-9

実験手法

X-RAY DIFFRACTION (2.83 Å)