ATPases associated with diverse cellular activities (AAA+ proteins) are a superfamily of
proteins found throughout all domains of life. The hallmark of this family is a conserved …

The biological diversity of the unicellular bacteria—whether assessed by shape, food,
metabolism, or ecological niche—surely rivals (if not exceeds) that of the multicellular …

Single particle cryo-EM excels in determining static structures of protein molecules, but
existing 3D reconstruction methods have been ineffective in modelling flexible proteins. We …

ClpXP is an ATP-dependent protease in which the ClpX AAA+ motor binds, unfolds, and
translocates specific protein substrates into the degradation chamber of ClpP. We present …

The 26S proteasome is the most complex ATP-dependent protease machinery, of~ 2.5 MDa
mass, ubiquitously found in all eukaryotes. It selectively degrades ubiquitin-conjugated …

Mitochondrial ClpP is a serine protease located in the mitochondrial matrix. This protease
participates in mitochondrial protein quality control by degrading misfolded or damaged …

The Holliday junction is a key intermediate formed during DNA recombination across all
kingdoms of life. In bacteria, the Holliday junction is processed by two homo-hexameric …

ClpP is a highly conserved serine protease that is a critical enzyme in maintaining protein
homeostasis and is an important drug target in pathogenic bacteria and various cancers. In …

When ribosomes fail to complete normal translation, all cells have mechanisms to ensure
degradation of the resulting partial proteins to safeguard proteome integrity. In Escherichia …

The ClpAP complex is a conserved bacterial protease that unfolds and degrades proteins
targeted for destruction. The ClpA double-ring hexamer powers substrate unfolding and …