6WQH

Molecular basis for the ATPase-powered substrate translocation by the Lon AAA+ protease

Summary for 6WQH

• Entry DOI: 10.2210/pdb6wqh/pdb
• EMDB information: 21870
• Descriptor: Lon protease, Ig2 substrate, PHOSPHOTHIOPHOSPHORIC ACID-ADENYLATE ESTER, ... (5 entities in total)
• Functional Keywords: lon aaa+, protease, cryo-em, dual pore-loops, motor protein
• Biological source: Meiothermus taiwanensis; More
• Total number of polymer chains: 7
• Total formula weight: 538098.43

Authors

Zhang, K.,Li, S.,Hsiehb, K.,Sub, S.,Pintilie, G.,Chiu, W.,Chang, C. (deposition date: 2020-04-28, release date: 2021-06-09, Last modification date: 2024-10-16)

Primary citation

Li, S.,Hsieh, K.Y.,Su, S.C.,Pintilie, G.D.,Zhang, K.,Chang, C.I.
Molecular basis for ATPase-powered substrate translocation by the Lon AAA+ protease.
J.Biol.Chem., 297:101239-101239, 2021

PubMed 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 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.

PubMed: 34563541
DOI: 10.1016/j.jbc.2021.101239

Experimental method

ELECTRON MICROSCOPY (3.6 Å)