Abstract
The AAA (ATPases associated with various cellular activities) protein family encompasses a large and diverse group of enzymes that are able to induce structural changes in a wide range of substrate proteins and protein complexes. The family's defining feature is an extended and highly conserved ATPase module that combines a core P-loop NTPase domain with a carboxy-terminal four-helical bundle. AAA proteins assemble into oligomeric rings and undergo conformational changes during cycles of nucleotide binding and hydrolysis. These concerted changes typically direct unfolding or remodeling of the bound substrates. As their name implies, AAA proteins perform a wide variety of cellular functions. This functional versatility is primarily based on idiosyncratic substrate-recognition domains that allow each member of the AAA protein family to interact with a distinct set of substrate proteins. As a consequence, AAA proteins can mediate diverse processes such as protein unfolding and degradation, vesicle transport, organelle assembly, and membrane dynamics.
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