Abstract
HtrA proteases can switch between active and inactive states to adjust their enzymatic activity to the needs of the cell. Structural and biochemical studies of bacterial DegP show that peptide binding to the PDZ domain of DegP induces the conversion of resting hexameric DegP into active higher-order DegP complexes. A specific protease loop in the 12- and 24-meric DegP particles senses the relocated PDZ domain, inducing conformational changes that ultimately result in protease activation.
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