› 3wu6

X-ray diffraction
1.8Å resolution

Oxidized E.coli Lon Proteolytic domain

Released:
DOI: 10.2210/pdb3wu6/pdb
PDB entry 3wu6 coloured by chain, front view.
PDB entry 3wu6 coloured by chain, side view.
PDB entry 3wu6 coloured by chain, top view.
Source organism: Escherichia coli DH1
Primary publication:
A redox switch shapes the Lon protease exit pore to facultatively regulate proteolysis.
Nishii W, Kukimoto-Niino M, Terada T, Shirouzu M, Muramatsu T, Kojima M, Kihara H, Yokoyama S
Nat Chem Biol 11 46-51 (2015)
PMID: 25383757

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assemblies composition:
homo hexamer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-164236 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 200 amino acids
Theoretical weight: 21.37 KDa
Source organism: Escherichia coli DH1
Expression system: Escherichia coli
Structure domains: Ribosomal Protein S5; domain 2

Ligands and Environments

1 bound ligand:
Ligand SO4 5 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B2
Spacegroup: P31
Unit cell:
a: 86.438Å b: 86.438Å c: 124.936Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.191 0.189 0.226
Expression system: Escherichia coli

Quick links

Citations

5 review citations

Allosteric disulfides: Sophisticated molecular structures enabling flexible protein regulation.
Chiu et al. (2019)
4 more