3GDU

Crystal structure of DegS H198P/D320A mutant modified by DFP and in complex with YRF peptide

Summary for 3GDU

• Entry DOI: 10.2210/pdb3gdu/pdb
• Related: 3GDS 3GDV
• Descriptor: DegS protease, YRF peptide (2 entities in total)
• Functional Keywords: protease, stress-sensor, htra, pdz omp, hydrolase, periplasm, serine protease, hydrolase-hydrolase activator complex, hydrolase/hydrolase activator
• Biological source: Escherichia Coli
• Cellular location: Cell inner membrane ; Single-pass membrane protein : P0AEE3
• Total number of polymer chains: 6
• Total formula weight: 110230.04

Authors

Sohn, J.,Grant, R.A.,Sauer, R.T. (deposition date: 2009-02-24, release date: 2009-03-31, Last modification date: 2021-10-20)

Primary citation

Sohn, J.,Grant, R.A.,Sauer, R.T.
OMP peptides activate the DegS stress-sensor protease by a relief of inhibition mechanism.
Structure, 17:1411-1421, 2009

PubMed Abstract: In the E. coli periplasm, C-terminal peptides of misfolded outer-membrane porins (OMPs) bind to the PDZ domains of the trimeric DegS protease, triggering cleavage of a transmembrane regulator and transcriptional activation of stress genes. We show that an active-site DegS mutation partially bypasses the requirement for peptide activation and acts synergistically with mutations that disrupt contacts between the protease and PDZ domains. Biochemical results support an allosteric model, in which these mutations, active-site modification, and peptide/substrate binding act in concert to stabilize proteolytically active DegS. Cocrystal structures of DegS in complex with different OMP peptides reveal activation of the protease domain with varied conformations of the PDZ domain and without specific contacts from the bound OMP peptide. Taken together, these results indicate that the binding of OMP peptides activates proteolysis principally by relieving inhibitory contacts between the PDZ domain and the protease domain of DegS.

PubMed: 19836340
DOI: 10.1016/j.str.2009.07.017

Experimental method

X-RAY DIFFRACTION (3 Å)