› 1vcw

X-ray diffraction
3.05Å resolution

Crystal structure of DegS after backsoaking the activating peptide

Released:
DOI: 10.2210/pdb1vcw/pdb
PDB entry 1vcw coloured by chain, front view.
PDB entry 1vcw coloured by chain, side view.
PDB entry 1vcw coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the DegS stress sensor: How a PDZ domain recognizes misfolded protein and activates a protease.
Wilken C, Kitzing K, Kurzbauer R, Ehrmann M, Clausen T
Cell 117 483-94 (2004)
PMID: 15137941

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 domains:

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: 314 amino acids
Theoretical weight: 33.24 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEE3 (Residues: 43-355; Coverage: 88%)
Gene names: JW3204, b3235, degS, hhoB, htrH
Sequence domains:
Structure domains:

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: C2
Unit cell:
a: 206.99Å b: 142.733Å c: 41.231Å
α: 90° β: 90.09° γ: 90°
R-values:
R R work R free
0.235 0.233 0.301
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

39 review citations

HTRA proteases: regulated proteolysis in protein quality control.
Clausen et al. (2011)
38 more

3 mentions without citation

Membrane proteases in the bacterial protein secretion and quality control pathway.
Dalbey et al. (2012)
2 more