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• W2989594468 abstract "Abstract The ClpP protease is found in all kingdoms of life, from bacteria to humans. In general, this protease forms a homo-oligomeric complex composed of 14 identical subunits, which associates with its cognate ATPase in a symmetrical manner. Here we show that, in contrast to this general architecture, the Clp protease from Mycobacterium smegmatis ( Msm ) forms an asymmetric hetero-oligomeric complex ClpP1P2, which only associates with its cognate ATPase through the ClpP2 ring. Our structural and functional characterisation of this complex demonstrates that asymmetric docking of the ATPase component is controlled by both the composition of the ClpP1 hydrophobic pocket (Hp) and the presence of a unique C-terminal extension in ClpP1 that guards this Hp. Our structural analysis of Msm ClpP1 also revealed openings in the side-walls of the inactive tetradecamer, which may represent sites for product egress." @default.
• W2989594468 created "2019-12-05" @default.
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• W2989594468 date "2019-12-02" @default.
• W2989594468 modified "2023-10-17" @default.
• W2989594468 title "Molecular and structural insights into an asymmetric proteolytic complex (ClpP1P2) from Mycobacterium smegmatis" @default.
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• W2989594468 doi "https://doi.org/10.1038/s41598-019-53736-8" @default.
• W2989594468 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/6889138" @default.
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• W2989594468 hasPublicationYear "2019" @default.
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