3H4M

AAA ATPase domain of the proteasome- activating nucleotidase

3H4M の概要

• エントリーDOI: 10.2210/pdb3h4m/pdb
• 関連するPDBエントリー: 3H43 3H4P
• 分子名称: Proteasome-activating nucleotidase, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
• 機能のキーワード: atpase, proteasome, pan, atp-binding, nucleotide-binding, hydrolase
• 由来する生物種: Methanocaldococcus jannaschii (Methanococcus jannaschii)
• 細胞内の位置: Cytoplasm: Q58576
• タンパク質・核酸の鎖数: 3
• 化学式量合計: 97387.51

構造登録者

Jeffrey, P.,Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Shi, Y. (登録日: 2009-04-20, 公開日: 2009-06-09, 最終更新日: 2024-02-21)

主引用文献

Zhang, F.,Hu, M.,Tian, G.,Zhang, P.,Finley, D.,Jeffrey, P.D.,Shi, Y.
Structural Insights into the Regulatory Particle of the Proteasome from Methanocaldococcus jannaschii.
Mol.Cell, 34:473-484, 2009

PubMed Abstract: Eukaryotic proteasome consists of a core particle (CP), which degrades unfolded protein, and a regulatory particle (RP), which is responsible for recognition, ATP-dependent unfolding, and translocation of polyubiquitinated substrate protein. In the archaea Methanocaldococcus jannaschii, the RP is a homohexameric complex of proteasome-activating nucleotidase (PAN). Here, we report the crystal structures of essential elements of the archaeal proteasome: the CP, the ATPase domain of PAN, and a distal subcomplex that is likely the first to encounter substrate. The distal subcomplex contains a coiled-coil segment and an OB-fold domain, both of which appear to be conserved in the eukaryotic proteasome. The OB domains of PAN form a hexameric ring with a 13 A pore, which likely constitutes the outermost constriction of the substrate translocation channel. These studies reveal structural codes and architecture of the complete proteasome, identify potential substrate-binding sites, and uncover unexpected asymmetry in the RP of archaea and eukaryotes.

PubMed: 19481527
DOI: 10.1016/j.molcel.2009.04.021

実験手法

X-RAY DIFFRACTION (3.106 Å)