› 6n2i

X-ray diffraction
3.5Å resolution

Lon protease AAA+ domain

Released:
DOI: 10.2210/pdb6n2i/pdb
PDB entry 6n2i coloured by chain, front view.
PDB entry 6n2i coloured by chain, side view.
PDB entry 6n2i coloured by chain, top view.
Source organism: Escherichia coli
Primary publication:
New insights into structural and functional relationships between LonA proteases and ClpB chaperones.
Rotanova TV, Andrianova AG, Kudzhaev AM, Li M, Botos I, Wlodawer A, Gustchina A
FEBS Open Bio 9 1536-1551 (2019)
PMID: 31237118

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: 344 amino acids
Theoretical weight: 38.8 KDa
Source organism: Escherichia coli
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P0A9M0 (Residues: 241-584; Coverage: 44%)
Gene names: JW0429, b0439, capR, deg, lon, lopA, muc
Sequence domains: ATPase family associated with various cellular activities (AAA)

Ligands and Environments

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

Experiments and Validation Details

Entry percentile scores
X-ray source: APS BEAMLINE 22-ID
Spacegroup: P65
Unit cell:
a: 88.6Å b: 88.6Å c: 67.74Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.287 0.284 0.325
Expression system: Escherichia coli BL21

Quick links

Citations

2 review citations

The ins and outs of Bacillus proteases: activities, functions and commercial significance.
Harwood et al. (2022)
1 more

4 mentions without citation

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