7CRA

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

Summary for 7CRA

• Entry DOI: 10.2210/pdb7cra/pdb
• Descriptor: Lon protease, SULFATE ION (3 entities in total)
• Functional Keywords: lon protease, aaa+ protein, hydrolase
• Biological source: Meiothermus taiwanensis
• Total number of polymer chains: 1
• Total formula weight: 33562.39

Authors

Lin, C.-C.,Chang, C.-I. (deposition date: 2020-08-13, release date: 2021-05-26, Last modification date: 2023-11-29)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (1.7 Å)