› 1te0

X-ray diffraction
2.2Å resolution

Structural analysis of DegS, a stress sensor of the bacterial periplasm

Released:
DOI: 10.2210/pdb1te0/pdb
PDB entry 1te0 coloured by chain, front view.
PDB entry 1te0 coloured by chain, side view.
PDB entry 1te0 coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Structural analysis of DegS, a stress sensor of the bacterial periplasm.
Zeth K
FEBS Lett 569 351-8 (2004)
PMID: 15225661

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:
Sequence domains:
Structure domains:

Structure analysis Details

Assemblies composition:
homo trimer (preferred)
homo 24-mer
Assembly name:
PDBe Complex ID:
PDB-CPX-142438 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Serine endoprotease DegS Chains: A, B
Molecule details ›
Chains: A, B
Length: 318 amino acids
Theoretical weight: 33.69 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P0AEE3 (Residues: 37-354; Coverage: 90%)
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: ESRF BEAMLINE ID14-4
Spacegroup: I23
Unit cell:
a: 166.28Å b: 166.28Å c: 166.28Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.247 0.245 0.295
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

6 review citations

The mitochondrial serine protease HtrA2/Omi: an overview.
Vande Walle et al. (2008)
5 more

7 mentions without citation

Function, molecular mechanisms, and therapeutic potential of bacterial HtrA proteins: An evolving view.
Song et al. (2022)
6 more