› 3ljc

X-ray diffraction
2.6Å resolution

Crystal structure of Lon N-terminal domain.

Released:
DOI: 10.2210/pdb3ljc/pdb
PDB entry 3ljc coloured by chain, front view.
PDB entry 3ljc coloured by chain, side view.
PDB entry 3ljc coloured by chain, top view.
Source organism: Escherichia coli K-12
Primary publication:
Structure of the N-terminal fragment of Escherichia coli Lon protease.
Li M, Gustchina A, Rasulova FS, Melnikov EE, Maurizi MR, Rotanova TV, Dauter Z, Wlodawer A
Acta Crystallogr D Biol Crystallogr 66 865-73 (2010)
PMID: 20693685

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:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-141896 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease Chain: A
Molecule details ›
Chain: A
Length: 252 amino acids
Theoretical weight: 29.57 KDa
Source organism: Escherichia coli K-12
Expression system: Escherichia coli
UniProt:
  • Canonical: P0A9M0 (Residues: 1-245; Coverage: 31%)
Gene names: JW0429, b0439, capR, deg, lon, lopA, muc
Sequence domains: ATP-dependent protease La (LON) substrate-binding domain
Structure domains:

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 14 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P3221
Unit cell:
a: 91.568Å b: 91.568Å c: 81.862Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.235 0.233 0.282
Expression system: Escherichia coli

Quick links

Citations

3 review citations

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

15 mentions without citation

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