{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"omics_type":["Unknown"],"volume":["7(42)"],"submitter":["Li S"],"pubmed_abstract":["Lon is an evolutionarily conserved proteolytic machine carrying out a wide spectrum of biological activities by degrading misfolded damaged proteins and specific cellular substrates. Lon contains a large N-terminal domain and forms a hexameric core of fused adenosine triphosphatase and protease domains. Here, we report two complete structures of Lon engaging a substrate, determined by cryo–electron microscopy to 2.4-angstrom resolution. These structures show a multilayered architecture featuring a tensegrity triangle complex, uniquely constructed by six long N-terminal helices. The interlocked helix triangle is assembled on the top of the hexameric core to spread a web of six globular substrate-binding domains. It serves as a multipurpose platform that controls the access of substrates to "],"journal":["Science advances"],"pagination":["eabj7835"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8519571"],"repository":["biostudies-literature"],"pubmed_title":["Complete three-dimensional structures of the Lon protease translocating a protein substrate."],"pmcid":["PMC8519571"],"pubmed_authors":["Hsieh KY","Li S","Zhang K","Lee SH","Pintilie GD","Chang CI","Kuo CI"],"additional_accession":[]},"is_claimable":false,"name":"Complete three-dimensional structures of the Lon protease translocating a protein substrate.","description":"Lon is an evolutionarily conserved proteolytic machine carrying out a wide spectrum of biological activities by degrading misfolded damaged proteins and specific cellular substrates. Lon contains a large N-terminal domain and forms a hexameric core of fused adenosine triphosphatase and protease domains. Here, we report two complete structures of Lon engaging a substrate, determined by cryo–electron microscopy to 2.4-angstrom resolution. These structures show a multilayered architecture featuring a tensegrity triangle complex, uniquely constructed by six long N-terminal helices. The interlocked helix triangle is assembled on the top of the hexameric core to spread a web of six globular substrate-binding domains. It serves as a multipurpose platform that controls the access of substrates to ","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Oct","modification":"2026-05-08T15:50:36.303Z","creation":"2025-02-19T00:03:16.983Z"},"accession":"S-EPMC8519571","cross_references":{"pubmed":["34652947"],"doi":["10.1126/sciadv.abj7835"]}}