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Abstract
The effect of the coiled-coil (CC) region of the α-helical inserted domain of Escherichia coli Lon protease (Ec-Lon) on the functional activity of the enzyme has been characterized. A recombinant form des-CC(G5)-Lon in which the deleted CC fragment is replaced by a pentaglycine peptide has been obtained and investigated. It has been shown that the CC region is involved in the recognition of the nucleotide nature by the enzyme and the interaction of the enzyme with the protein substrate. It has been also established that the CC region is necessary for the formation and functioning of the ATPase and peptidase active centers, the occurrence of allosteric interactions between them, and for the implementation of proteolysis by a unique processive mechanism.
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