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TitleStructural and mechanistic studies on human LONP1 redefine the hand-over-hand translocation mechanism.
Journal, issue, pagesbioRxiv, Year 2024
Publish dateJun 25, 2024
AuthorsJeffrey T Mindrebo / Gabriel C Lander /
PubMed AbstractAAA+ enzymes use energy from ATP hydrolysis to remodel diverse cellular targets. Structures of substrate-bound AAA+ complexes suggest that these enzymes employ a conserved hand-over-hand mechanism to ...AAA+ enzymes use energy from ATP hydrolysis to remodel diverse cellular targets. Structures of substrate-bound AAA+ complexes suggest that these enzymes employ a conserved hand-over-hand mechanism to thread substrates through their central pore. However, the fundamental aspects of the mechanisms governing motor function and substrate processing within specific AAA+ families remain unresolved. We used cryo-electron microscopy to structurally interrogate reaction intermediates from in vitro biochemical assays to inform the underlying regulatory mechanisms of the human mitochondrial AAA+ protease, LONP1. Our results demonstrate that substrate binding allosterically regulates proteolytic activity, and that LONP1 can adopt a configuration conducive to substrate translocation even when the ATPases are bound to ADP. These results challenge the conventional understanding of the hand-over-hand translocation mechanism, giving rise to an alternative model that aligns more closely with biochemical and biophysical data on related enzymes like ClpX, ClpA, the 26S proteasome, and Lon protease.
External linksbioRxiv / PubMed:38979310 / PubMed Central
MethodsEM (single particle)
Resolution3.18 - 3.31 Å
Structure data

45430

9cc0

EMDB-45430, PDB-9cc0:
Human Mitochondrial LONP1 Degrading Casein, ATP-bound closed form
Method: EM (single particle) / Resolution: 3.31 Å

45433

9cc3

EMDB-45433, PDB-9cc3:
Human Mitochondrial LONP1 Stall State + casein
Method: EM (single particle) / Resolution: 3.23 Å

EMDB-45434: LONP1 stall state bound to substrate and 4 ADPs
Method: EM (single particle) / Resolution: 3.18 Å

Chemicals

ChemComp-ATP:
ADENOSINE-5'-TRIPHOSPHATE / ATP, energy-carrying molecule*YM

ChemComp-MG:
Unknown entry

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

Source
  • homo sapiens (human)
  • bos taurus (cattle)
  • escherichia coli 'bl21-gold(de3)plyss ag' (bacteria)
KeywordsHYDROLASE / ATPase / protease

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