2qf0

X-ray diffraction
2.5Å resolution

Structure of the delta PDZ truncation of the DegS protease

Released:
Source organism: Escherichia coli K-12
Primary publication:
Allosteric activation of DegS, a stress sensor PDZ protease.
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

Structure analysis Details

Assembly composition:
homo trimer (preferred)
PDBe Complex ID:
PDB-CPX-142438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine endoprotease DegS Chains: A, B, C, D, E, F, G, H, I
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I
Length: 243 amino acids
Theoretical weight: 26.32 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

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 24-ID-C
Spacegroup: P212121
Unit cell:
a: 72.168Å b: 132.974Å c: 229.33Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.207 0.207 0.257
Expression system: Escherichia coli