› 2ane

X-ray diffraction
2.03Å resolution

Crystal structure of N-terminal domain of E.Coli Lon Protease

Released:
DOI: 10.2210/pdb2ane/pdb
PDB entry 2ane coloured by chain, front view.
PDB entry 2ane coloured by chain, side view.
PDB entry 2ane coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
Crystal structure of the N-terminal domain of E. coli Lon protease.
Li M, Rasulova F, Melnikov EE, Rotanova TV, Gustchina A, Maurizi MR, Wlodawer A
Protein Sci 14 2895-900 (2005)
PMID: 16199667

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo octamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141898 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease Chains: A, B, C, D, E, F, G, H
Molecule details ›
Chains: A, B, C, D, E, F, G, H
Length: 125 amino acids
Theoretical weight: 14.1 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9M0 (Residues: 1-118; Coverage: 15%)
Gene names: JW0429, b0439, capR, deg, lon, lopA, muc
Sequence domains: ATP-dependent protease La (LON) substrate-binding domain
Structure domains: LON domain-like

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU
Spacegroup: P21
Unit cell:
a: 90.61Å b: 53.445Å c: 111.973Å
α: 90° β: 107.5° γ: 90°
R-values:
R R work R free
0.212 0.212 0.268
Expression system: Escherichia coli

Quick links

Citations

8 review citations

Mitochondrial protein oxidation and degradation in response to oxidative stress and aging.
Bulteau et al. (2006)
7 more

8 mentions without citation

Slicing a protease: structural features of the ATP-dependent Lon proteases gleaned from investigations of isolated domains.
Rotanova et al. (2006)
7 more