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The crystal structure of an ATP-independent LonC protease revealed a proteolytic chamber with two open axial pores. A LonC-specific N-­terminal coil tethers the AAA+ and protease domains together. Structures with covalent inhibitors bound to the proteolytic active sites provide mechanistic insights into the recognition of inhibitors and polypeptide substrates within the conserved Lon proteolytic chamber.

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The crystal structure of the intact substrate-recognition domain of a LonC protease shows a large helical hairpin extension (HHE). The HHEs form a basket-like structure on top of the degradation chamber of the LonC protease. The HHE of LonC shares structural and functional similarity to the α-helical tentacle of the periplasmic chaperone Skp.
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