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- W3021330807 abstract "Abstract 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 the substrate into a hexameric proteolytic chamber. To understand the structural basis for the substrate translocation process, we have determined the cryo-electron microscopy (cryo-EM) structure of Meiothermus taiwanensis LonA (MtaLonA) at 3.6 Å resolution in a substrate-engaged state. 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; a closed AAA+ ring is nevertheless maintained by two disengaged ADP-bound protomers transiting between the lowest and highest position. The 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." @default.
- W3021330807 created "2020-05-13" @default.
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- W3021330807 date "2020-04-30" @default.
- W3021330807 modified "2023-10-14" @default.
- W3021330807 title "Molecular basis for the ATPase-powered substrate translocation by the Lon AAA+ protease" @default.
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- W3021330807 doi "https://doi.org/10.1101/2020.04.29.068361" @default.
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