› 3mh6

X-ray diffraction
3.6Å resolution

HtrA proteases are activated by a conserved mechanism that can be triggered by distinct molecular cues

Released:
DOI: 10.2210/pdb3mh6/pdb
PDB entry 3mh6 coloured by chain, front view.
PDB entry 3mh6 coloured by chain, side view.
PDB entry 3mh6 coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
HtrA proteases have a conserved activation mechanism that can be triggered by distinct molecular cues.
Krojer T, Sawa J, Huber R, Clausen T
Nat Struct Mol Biol 17 844-52 (2010)
PMID: 20581825

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 analysis Details

Assembly composition:
homo 24-mer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-142920 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Periplasmic serine endoprotease DegP Chain: A
Molecule details ›
Chain: A
Length: 456 amino acids
Theoretical weight: 47.94 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0C0V0 (Residues: 27-474; Coverage: 100%)
Gene names: JW0157, b0161, degP, htrA, ptd
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand DFP 1 x DFP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SLS BEAMLINE X06SA
Spacegroup: F432
Unit cell:
a: 261.5Å b: 261.5Å c: 261.5Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.275 0.273 0.309
Expression system: Escherichia coli

Quick links

Citations

17 review citations

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

2 mentions without citation

Inhibiting Helicobacter pylori HtrA protease by addressing a computationally predicted allosteric ligand binding site.
Perna et al. (2014)
1 more