› 3m6a

X-ray diffraction
3.4Å resolution

Crystal structure of Bacillus subtilis Lon C-terminal domain

Released:
DOI: 10.2210/pdb3m6a/pdb
PDB entry 3m6a coloured by chain, front view.
PDB entry 3m6a coloured by chain, side view.
PDB entry 3m6a coloured by chain, top view.
Source organism: Bacillus subtilis subsp. subtilis str. 168
Primary publication:
Crystal structures of Bacillus subtilis Lon protease.
Duman RE, Löwe J
J Mol Biol 401 653-70 (2010)
PMID: 20600124

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

Assemblies composition:
homo hexamer
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153516 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease 1 Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 543 amino acids
Theoretical weight: 60.04 KDa
Source organism: Bacillus subtilis subsp. subtilis str. 168
Expression system: Escherichia coli
UniProt:
  • Canonical: P37945 (Residues: 240-774; Coverage: 69%)
Gene names: BSU28200, lon1, lonA
Sequence domains:
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 6 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID23-1
Spacegroup: P21
Unit cell:
a: 103.382Å b: 127.4Å c: 148.993Å
α: 90° β: 100.5° γ: 90°
R-values:
R R work R free
0.267 0.265 0.313
Expression system: Escherichia coli

Quick links

Citations

6 review citations

AAA+ proteases: ATP-fueled machines of protein destruction.
Sauer et al. (2011)
5 more

12 mentions without citation

Multitasking in the mitochondrion by the ATP-dependent Lon protease.
Venkatesh et al. (2012)
11 more