7FID

Processive cleavage of substrate at individual proteolytic active sites of the Lon proteasecomplex (conformation 1)

7FID の概要

• エントリーDOI: 10.2210/pdb7fid/pdb
• EMDBエントリー: 31589
• 分子名称: Lon protease, unknown endogenous substrate, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (4 entities in total)
• 機能のキーワード: aaa, protease, complex, proteolysis, hydrolase
• 由来する生物種: Meiothermus taiwanensis; 詳細
• タンパク質・核酸の鎖数: 7
• 化学式量合計: 545229.68

構造登録者

Li, S.,Hsieh, K.,Kuo, C.,Su, S.,Huang, K.,Zhang, K.,Chang, C.I. (登録日: 2021-07-31, 公開日: 2021-11-24, 最終更新日: 2025-07-02)

主引用文献

Li, S.,Hsieh, K.Y.,Kuo, C.I.,Su, S.C.,Huang, K.F.,Zhang, K.,Chang, C.I.
Processive cleavage of substrate at individual proteolytic active sites of the Lon protease complex.
Sci Adv, 7:eabj9537-eabj9537, 2021

PubMed Abstract: The Lon protease is the prototype of a family of proteolytic machines with adenosine triphosphatase modules built into a substrate degradation chamber. Lon is known to degrade protein substrates in a processive fashion, cutting a protein chain processively into small peptides before commencing cleavages of another protein chain. Here, we present structural and biochemical evidence demonstrating that processive substrate degradation occurs at each of the six proteolytic active sites of Lon, which forms a deep groove that partially encloses the substrate polypeptide chain by accommodating only the unprimed residues and permits processive cleavage in the C-to-N direction. We identify a universally conserved acidic residue at the exit side of the binding groove indispensable for the proteolytic activity. This noncatalytic residue likely promotes processive proteolysis by carboxyl-carboxylate interactions with cleaved intermediates. Together, these results uncover a previously unrecognized mechanism for processive substrate degradation by the Lon protease.

PubMed: 34757797
DOI: 10.1126/sciadv.abj9537

実験手法

ELECTRON MICROSCOPY (2.44 Å)