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8OKA

Human Mitochondrial Lon Y394F Mutant ADP Bound

これはPDB形式変換不可エントリーです。
8OKA の概要
エントリーDOI10.2210/pdb8oka/pdb
関連するPDBエントリー8OJL
EMDBエントリー16923
分子名称Lon protease homolog, mitochondrial, ADENOSINE-5'-DIPHOSPHATE (2 entities in total)
機能のキーワードhuman mitochondrial aaa+ protease, motor protein, hydrolase
由来する生物種Homo sapiens (human)
タンパク質・核酸の鎖数6
化学式量合計591666.32
構造登録者
Kereiche, S.,Bauer, J.A.,Matyas, P.,Novacek, J.,Kutejova, E. (登録日: 2023-03-28, 公開日: 2024-04-10, 最終更新日: 2024-05-15)
主引用文献Kunova, N.,Ondrovicova, G.,Bauer, J.A.,Krajcovicova, V.,Pinkas, M.,Stojkovicova, B.,Havalova, H.,Lukacova, V.,Kohutova, L.,Kostan, J.,Martinakova, L.,Barath, P.,Novacek, J.,Zoll, S.,Kereiche, S.,Kutejova, E.,Pevala, V.
Polyphosphate and tyrosine phosphorylation in the N-terminal domain of the human mitochondrial Lon protease disrupts its functions.
Sci Rep, 14:9923-9923, 2024
Cited by
PubMed Abstract: Phosphorylation plays a crucial role in the regulation of many fundamental cellular processes. Phosphorylation levels are increased in many cancer cells where they may promote changes in mitochondrial homeostasis. Proteomic studies on various types of cancer identified 17 phosphorylation sites within the human ATP-dependent protease Lon, which degrades misfolded, unassembled and oxidatively damaged proteins in mitochondria. Most of these sites were found in Lon's N-terminal (NTD) and ATPase domains, though little is known about the effects on their function. By combining the biochemical and cryo-electron microscopy studies, we show the effect of Tyr186 and Tyr394 phosphorylations in Lon's NTD, which greatly reduce all Lon activities without affecting its ability to bind substrates or perturbing its tertiary structure. A substantial reduction in Lon's activities is also observed in the presence of polyphosphate, whose amount significantly increases in cancer cells. Our study thus provides an insight into the possible fine-tuning of Lon activities in human diseases, which highlights Lon's importance in maintaining proteostasis in mitochondria.
PubMed: 38688959
DOI: 10.1038/s41598-024-60030-9
主引用文献が同じPDBエントリー
実験手法
ELECTRON MICROSCOPY (3.89 Å)
構造検証レポート
Validation report summary of 8oka
検証レポート(詳細版)ダウンロードをダウンロード

227561

件を2024-11-20に公開中

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