› 2qf3

X-ray diffraction
2.04Å resolution

Structure of the delta PDZ truncation of the DegS protease

Released:
DOI: 10.2210/pdb2qf3/pdb
PDB entry 2qf3 coloured by chain, front view.
PDB entry 2qf3 coloured by chain, side view.
PDB entry 2qf3 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Allosteric activation of DegS, a stress sensor PDZ protease.
Sohn J, Grant RA, Sauer RT
Cell 131 572-83 (2007)
PMID: 17981123

Function and Biology Details

Reaction catalysed: 
Acts on substrates that are at least partially unfolded. The cleavage site P1 residue is normally between a pair of hydrophobic residues, such as Val-|-Val
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo trimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine endoprotease DegS Chains: A, B, C
Molecule details ›
Chains: A, B, C
Length: 243 amino acids
Theoretical weight: 26.13 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0AEE3 (Residues: 27-256; Coverage: 65%)
Gene names: JW3204, b3235, degS, hhoB, htrH
Sequence domains: Trypsin
Structure domains: Trypsin-like serine proteases

Ligands and Environments

1 bound ligand:
Ligand PO4 3 x PO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU MICROMAX-007 HF
Spacegroup: P212121
Unit cell:
a: 72.347Å b: 75.316Å c: 162.257Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.189 0.189 0.219
Expression system: Escherichia coli

Quick links

Citations

18 review citations

β-Barrel membrane protein assembly by the Bam complex.
Hagan et al. (2011)
17 more

2 mentions without citation

Allostery is an intrinsic property of the protease domain of DegS: implications for enzyme function and evolution.
Sohn et al. (2010)
1 more