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TitleStructural Analysis of Human LonP1 Protease Bound with the Native Substrate.
Journal, issue, pagesLife (Basel), Vol. 16, Issue 3, Year 2026
Publish dateMar 16, 2026
AuthorsMing Li / Hongwei Liu / Shengchun Zhang / Qijun Gao / Shanshan Li / Junfeng Wang / Kaiming Zhang /
PubMed AbstractThe human mitochondrial Lon protease (LonP1) is a central regulator of mitochondrial DNA copy number and metabolic reprogramming. However, the structural basis for how LonP1 recognizes native ...The human mitochondrial Lon protease (LonP1) is a central regulator of mitochondrial DNA copy number and metabolic reprogramming. However, the structural basis for how LonP1 recognizes native physiological substrates remains elusive. Here, we present the high-resolution cryo-EM structure of the human LonP1 hexamer actively engaging its native substrate, TFAM. The reconstruction reveals a distinct bipartite search-and-shred mechanism. Unlike its bacterial homologs, the human N-terminal domain (NTD) adopts a compact architecture acting as a selective vestibule to recruit and initially unfold the substrate tertiary structure. Subsequently, the polypeptide is threaded through the central channel via a hand-over-hand mechanism driven by a spiral array of aromatic pore-loops. This structural framework provides a mechanistic rationale for the spatial segregation of LonP1 and offers a template for targeting mitochondrial proteostasis in human diseases.
External linksLife (Basel) / PubMed:41900996 / PubMed Central
MethodsEM (single particle)
Resolution3.22 Å
Structure data

68281

22ib

EMDB-68281, PDB-22ib:
CryoEM structure of Human LonP1-TFAM complex
Method: EM (single particle) / Resolution: 3.22 Å

Chemicals

ChemComp-AGS:
PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER / ATP-gamma-S, energy-carrying molecule analogue*YM

ChemComp-ADP:
ADENOSINE-5'-DIPHOSPHATE / ADP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

Source
  • homo sapiens (human)
KeywordsSTRUCTURAL PROTEIN / Human Lon protease / Complex

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