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Molecular basis for the ATPase-powered substrate translocation by the Lon AAA+ protease
bioRxiv - Biophysics Pub Date : 2021-09-16 , DOI: 10.1101/2020.04.29.068361 Shanshan Li , Kan-Yen Hsieh , Shih-Chieh Su , Grigore D. Pintilie , Kaiming Zhang , Chung-I Chang
bioRxiv - Biophysics Pub Date : 2021-09-16 , DOI: 10.1101/2020.04.29.068361 Shanshan Li , Kan-Yen Hsieh , Shih-Chieh Su , Grigore D. Pintilie , Kaiming Zhang , Chung-I Chang
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.
更新日期：2021-09-19
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