› 4fwg

X-ray diffraction
1.99Å resolution

Crystal structure of the Lon-like protease MtaLonC in complex with lactacystin

Released:
DOI: 10.2210/pdb4fwg/pdb
PDB entry 4fwg coloured by chain, front view.
PDB entry 4fwg coloured by chain, side view.
PDB entry 4fwg coloured by chain, top view.
Source organism: Meiothermus taiwanensis
Primary publication:
Structures of an ATP-independent Lon-like protease and its complexes with covalent inhibitors.
Liao JH, Ihara K, Kuo CI, Huang KF, Wakatsuki S, Wu SH, Chang CI
Acta Crystallogr D Biol Crystallogr 69 1395-402 (2013)
PMID: 23897463

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 hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-111860 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
endopeptidase La Chain: A
Molecule details ›
Chain: A
Length: 732 amino acids
Theoretical weight: 81.07 KDa
Source organism: Meiothermus taiwanensis
Expression system: Escherichia coli
UniProt:
  • Canonical: C9DRU9 (Residues: 1-719; Coverage: 100%)
Gene names: Mcate_02721, lon_2
Sequence domains:
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SLA 1 x SLA
Ligand PO4 1 x PO4
1 modified residue:
Ligand MSE 10 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL44XU
Spacegroup: P6
Unit cell:
a: 115.987Å b: 115.987Å c: 135.054Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.231 0.23 0.259
Expression system: Escherichia coli

Quick links

Citations

12 citation in other articles

Structural Basis for the Magnesium-Dependent Activation and Hexamerization of the Lon AAA+ Protease.
Su et al. (2016)
11 more

1 mention without citation

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