The inner cavity of Escherichia coli DegP protein is not essential for molecular chaperone and proteolytic activity.

ABSTRACT: The Escherichia coli DegP protein is an essential periplasmic protein for bacterial survival at high temperatures. DegP has the unusual property of working as a chaperone below 28 degrees C, but efficiently degrading unfolded proteins above 28 degrees C. Monomeric DegP contains a protease domain and two PDZ domains. It oligomerizes into a hexameric cage through the staggered association of trimers. The active sites are located in a central cavity that is only accessible laterally, and the 12 PDZ domains act as mobile sidewalls that mediate opening and closing of the gates. As access to the active sites is restricted, DegP is an example of a self-compartmentalized protease. To determine the essential elements of DegP that maintain the integrity of the hexameric cage, we constructed several

SUBMITTER: Jomaa A 

PROVIDER: S-EPMC1797295 | biostudies-literature | 2007 Feb

REPOSITORIES: biostudies-literature