Abstract
The recently discovered human mitochondrial AAA+ protein Skd3 (human CLPB) is a powerful disaggregase and its overall activity is impacted by disease-causing mutations. To establish mechanistic insights into Skd3 disaggregation activity, we used cryo-electron microscopy (cryo-EM) to capture a substrate-bound complex. We successfully determined a reconstruction of Skd3 bound to FITC-casein in which the AAA+ ring was well resolved. Through structural analysis, we resolve multiple oligomeric states of Skd3 including a canonical AAA+ hexamer and a non-canonical dodecameric state.
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