3STJ: Crystal Structure Of The Protease + Pdz1 Domain Of Degq From Escherichia Coli

Citation:
Abstract
To react to distinct stress situations and to prevent the accumulation of misfolded proteins, all cells employ a number of proteases and chaperones, which together set up an efficient protein quality control system. The functionality of proteins in the cell envelope of Escherichia coli is monitored by the HtrA proteases DegS, DegP, and DegQ. In contrast with DegP and DegS, the structure and function of DegQ has not been addressed in detail. Here, we show that substrate binding triggers the conversion of the resting DegQ hexamer into catalytically active 12- and 24-mers. Interestingly, substrate-induced oligomer reassembly and protease activation depends on the first PDZ domain but not on the second. Therefore, the regulatory mechanism originally identified in DegP should be a common feature of HtrA proteases, most of which encompass only a single PDZ domain. Using a DegQ mutant lacking the second PDZ domain, we determined the high resolution crystal structure of a dodecameric HtrA complex. The nearly identical domain orientation of protease and PDZ domains within 12- and 24-meric HtrA complexes reveals a conserved PDZ1 --> L3 --> LD/L1/L2 signaling cascade, in which loop L3 senses the repositioned PDZ1 domain of higher order, substrate-engaged particles and activates protease function. Furthermore, our in vitro and in vivo data imply a pH-related function of DegQ in the bacterial cell envelope.
PDB ID: 3STJDownload
MMDB ID: 93110
PDB Deposition Date: 2011/7/11
Updated in MMDB: 2011/08
Experimental Method:
x-ray diffraction
Resolution: 2.6  Å
Source Organism:
Escherichia coli K-12
Similar Structures:
Biological Unit for 3STJ: heptameric; determined by author and by software (PISA)
Molecular Components in 3STJ
Label Count Molecule
Proteins (7 molecules)
3
Protease Degq(Gene symbol: degQ)
Molecule annotation
4
Peptide (Unk)
Molecule annotation
* Click molecule labels to explore molecular sequence information.

Citing MMDB
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