7CRA

Crystal structure of the N-terminal fragment (residue 1-291) of LonA protease from Meiothermus taiwanensis

7CRA の概要

• エントリーDOI: 10.2210/pdb7cra/pdb
• 分子名称: Lon protease, SULFATE ION (3 entities in total)
• 機能のキーワード: lon protease, aaa+ protein, hydrolase
• 由来する生物種: Meiothermus taiwanensis
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 33562.39

構造登録者

Lin, C.-C.,Chang, C.-I. (登録日: 2020-08-13, 公開日: 2021-05-26, 最終更新日: 2023-11-29)

主引用文献

Tzeng, S.R.,Tseng, Y.C.,Lin, C.C.,Hsu, C.Y.,Huang, S.J.,Kuo, Y.T.,Chang, C.I.
Molecular insights into substrate recognition and discrimination by the N-terminal domain of Lon AAA+ protease.
Elife, 10:-, 2021

PubMed Abstract: The Lon AAA+ protease (LonA) is a ubiquitous ATP-dependent proteolytic machine, which selectively degrades damaged proteins or native proteins carrying exposed motifs (degrons). Here we characterize the structural basis for substrate recognition and discrimination by the N-terminal domain (NTD) of LonA. The results reveal that the six NTDs are attached to the hexameric LonA chamber by flexible linkers such that the formers tumble independently of the latter. Further spectral analyses show that the NTD selectively interacts with unfolded proteins, protein aggregates, and degron-tagged proteins by two hydrophobic patches of its N-lobe, but not intrinsically disordered substrate, α-casein. Moreover, the NTD selectively binds to protein substrates when they are thermally induced to adopt unfolded conformations. Collectively, our findings demonstrate that NTDs enable LonA to perform protein quality control to selectively degrade proteins in damaged states and suggest that substrate discrimination and selective degradation by LonA are mediated by multiple NTD interactions.

PubMed: 33929321
DOI: 10.7554/eLife.64056

実験手法

X-RAY DIFFRACTION (1.7 Å)