The complete three-dimensional structure of Lon protease is resolved

Science and Technology Daily News (Reporter Wu Changfeng) The reporter learned from the University of Science and Technology of China on October 20 that Zhang Kaiming's team from the Key Laboratory of Cell Dynamics of the Ministry of Education and collaborators worked together to analyze the complete three-dimensional structure of Lon protease and reveal its substrate.
The molecular mechanism of recognition and transfer, the research results were published in the journals "Journal of Biological Chemistry" and "Science Progress"
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Lon AAA+ protease (LonA) is an ATP-dependent protease that is conserved in the organelles of prokaryotes and eukaryotes
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Kaiming Zhang’s research team analyzed the cryo-EM structure of the substrate-bound state of Lon protease and found that the double-hole ring of the ATPase domain mediates the substrate interaction.
Four consecutive monomers in different ATP-bound and hydrolyzed states form a spiral ladder.
The arrangement reveals the molecular mechanism of continuous rotational translocation through LonA-specific allosteric
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The research results provide a complete framework for understanding the structural mechanism of Lon and other AAA+ proteases with similar activities