› 5e7s

X-ray diffraction
3.03Å resolution

Hexameric structure of a LonA protease domain in active state

Released:
DOI: 10.2210/pdb5e7s/pdb
PDB entry 5e7s coloured by chain, front view.
PDB entry 5e7s coloured by chain, side view.
PDB entry 5e7s coloured by chain, top view.
Source organism: Meiothermus taiwanensis
Primary publication:
Structural Basis for the Magnesium-Dependent Activation and Hexamerization of the Lon AAA+ Protease.
Su SC, Lin CC, Tai HC, Chang MY, Ho MR, Babu CS, Liao JH, Wu SH, Chang YC, Lim C, Chang CI
Structure 24 676-686 (2016)
PMID: 27041593

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 dodecamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-100266 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease Chains: A, B, C, D, E, F, G, H, I, J, K, L
Molecule details ›
Chains: A, B, C, D, E, F, G, H, I, J, K, L
Length: 298 amino acids
Theoretical weight: 32.6 KDa
Source organism: Meiothermus taiwanensis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A059VAZ3 (Residues: 491-781; Coverage: 37%)
Gene names: Mcate_02015, lon, lon1_1, lonA1
Sequence domains: Lon protease (S16) C-terminal proteolytic domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL15A1
Spacegroup: C2
Unit cell:
a: 116.309Å b: 212.787Å c: 178.921Å
α: 90° β: 100.8° γ: 90°
R-values:
R R work R free
0.23 0.227 0.279
Expression system: Escherichia coli

Quick links

Citations

2 review citations

Multifunctional Mitochondrial AAA Proteases.
Glynn SE. (2017)
1 more

1 mention without citation

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