6JPT

Crystal structure of human PAC3 homodimer (trigonal form)

6JPT の概要

• エントリーDOI: 10.2210/pdb6jpt/pdb
• 関連するPDBエントリー: 2Z5E
• 分子名称: Proteasome assembly chaperone 3, THIOCYANATE ION, POTASSIUM ION, ... (4 entities in total)
• 機能のキーワード: proteasome assembly chaperone, chaperone
• 由来する生物種: Homo sapiens (Human)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 13215.62

構造登録者

Satoh, T.,Yagi-Utsumi, M.,Okamoto, K.,Kurimoto, E.,Tanaka, K.,Kato, K. (登録日: 2019-03-27, 公開日: 2019-05-29, 最終更新日: 2023-11-22)

主引用文献

Satoh, T.,Yagi-Utsumi, M.,Okamoto, K.,Kurimoto, E.,Tanaka, K.,Kato, K.
Molecular and Structural Basis of the Proteasome alpha Subunit Assembly Mechanism Mediated by the Proteasome-Assembling Chaperone PAC3-PAC4 Heterodimer.
Int J Mol Sci, 20:-, 2019

PubMed Abstract: The 26S proteasome is critical for the selective degradation of proteins in eukaryotic cells. This enzyme complex is composed of approximately 70 subunits, including the structurally homologous proteins α1-α7, which combine to form heptameric rings. The correct arrangement of these α subunits is essential for the function of the proteasome, but their assembly does not occur autonomously. Assembly of the α subunit is assisted by several chaperones, including the PAC3-PAC4 heterodimer. In this study we showed that the PAC3-PAC4 heterodimer functions as a molecular matchmaker, stabilizing the α4-α5-α6 subcomplex during the assembly of the α-ring. We solved a 0.96-Å atomic resolution crystal structure for a PAC3 homodimer which, in conjunction with nuclear magnetic resonance (NMR) data, highlighted the mobility of the loop comprised of residues 51 to 61. Based on these structural and dynamic data, we created a three-dimensional model of the PAC3-4/α4/α5/α6 quintet complex, and used this model to investigate the molecular and structural basis of the mechanism of proteasome α subunit assembly, as mediated by the PAC3-PAC4 heterodimeric chaperone. Our results provide a potential basis for the development of selective inhibitors against proteasome biogenesis.

PubMed: 31067643
DOI: 10.3390/ijms20092231

実験手法

X-RAY DIFFRACTION (0.96 Å)