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TitleMolecular basis for ATPase-powered substrate translocation by the Lon AAA+ protease.
Journal, issue, pagesJ Biol Chem, Vol. 297, Issue 4, Page 101239, Year 2021
Publish dateSep 24, 2021
AuthorsShanshan Li / Kan-Yen Hsieh / Shih-Chieh Su / Grigore D Pintilie / Kaiming Zhang / Chung-I Chang /
PubMed AbstractThe Lon AAA+ (adenosine triphosphatases associated with diverse cellular activities) protease (LonA) converts ATP-fuelled conformational changes into sufficient mechanical force to drive ...The Lon AAA+ (adenosine triphosphatases associated with diverse cellular activities) protease (LonA) converts ATP-fuelled conformational changes into sufficient mechanical force to drive translocation of a substrate into a hexameric proteolytic chamber. To understand the structural basis for the substrate translocation process, we determined the cryo-electron microscopy (cryo-EM) structure of Meiothermus taiwanensis LonA (MtaLonA) in a substrate-engaged state at 3.6 Å resolution. Our data indicate that substrate interactions are mediated by the dual pore loops of the ATPase domains, organized in spiral staircase arrangement from four consecutive protomers in different ATP-binding and hydrolysis states. However, a closed AAA+ ring is maintained by two disengaged ADP-bound protomers transiting between the lowest and highest position. This structure reveals a processive rotary translocation mechanism mediated by LonA-specific nucleotide-dependent allosteric coordination among the ATPase domains, which is induced by substrate binding.
External linksJ Biol Chem / PubMed:34563541 / PubMed Central
MethodsEM (single particle)
Resolution3.6 Å
Structure data

21870

6wqh

EMDB-21870, PDB-6wqh:
Molecular basis for the ATPase-powered substrate translocation by the Lon AAA+ protease
Method: EM (single particle) / Resolution: 3.6 Å

Chemicals

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

ChemComp-4KZ:
N-[(1R)-1-(dihydroxyboranyl)-2-phenylethyl]-Nalpha-(pyrazin-2-ylcarbonyl)-L-phenylalaninamide

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

Source
  • meiothermus taiwanensis (bacteria)
  • dictyostelium discoideum (eukaryote)
KeywordsMOTOR PROTEIN / Lon AAA+ / protease / cryo-EM / dual pore-loops

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