› 4git

X-ray diffraction
2.88Å resolution

Crystal structure of alpha sub-domain of Lon protease from Brevibacillus thermoruber

Released:
DOI: 10.2210/pdb4git/pdb
PDB entry 4git coloured by chain, front view.
PDB entry 4git coloured by chain, side view.
PDB entry 4git coloured by chain, top view.
Source organism: Brevibacillus thermoruber
Primary publication:
Structural basis for DNA-mediated allosteric regulation facilitated by the AAA+ module of Lon protease.
Lee AY, Chen YD, Chang YY, Lin YC, Chang CF, Huang SJ, Wu SH, Hsu CH
Acta Crystallogr D Biol Crystallogr 70 218-30 (2014)
PMID: 24531457

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins in presence of ATP.
Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-183031 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease Chains: A, B
Molecule details ›
Chains: A, B
Length: 124 amino acids
Theoretical weight: 14.35 KDa
Source organism: Brevibacillus thermoruber
Expression system: Escherichia coli
UniProt:
  • Canonical: Q84FG5 (Residues: 491-605; Coverage: 15%)
Gene name: lon
Structure domains: Helicase, Ruva Protein; domain 3

Ligands and Environments

1 bound ligand:
Ligand SO4 2 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13C1
Spacegroup: P23
Unit cell:
a: 94.283Å b: 94.283Å c: 94.283Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.206 0.201 0.248
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways.
Muthuramalingam et al. (2016)
1 more

1 mention without citation

Structure and the Mode of Activity of Lon Proteases from Diverse Organisms.
Wlodawer et al. (2022)