› 8k3y

Electron Microscopy
4.42Å resolution

The "5+1" heteromeric structure of Lon protease consisting of a spiral pentamer with Y224S mutation and an N-terminal-truncated monomeric E613K mutant

Released:
DOI: 10.2210/pdb8k3y/pdb
PDB entry 8k3y coloured by chain, front view.
PDB entry 8k3y coloured by chain, side view.
PDB entry 8k3y coloured by chain, top view.
Source organism: Meiothermus taiwanensis
Primary publication:
A 5+1 assemble-to-activate mechanism of the Lon proteolytic machine.
Li S, Hsieh KY, Kuo CI, Lin TC, Lee SH, Chen YR, Wang CH, Ho MR, Ting SY, Zhang K, Chang CI
Nat Commun 14 7340 (2023)
PMID: 37957149
Related structures: EMD-36867

Function and Biology Details

Reaction catalysed: 
Hydrolysis of proteins in presence of ATP.
Biochemical function:
Biological process:
Cellular component:

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-232512 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Lon protease Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 799 amino acids
Theoretical weight: 89.31 KDa
Source organism: Meiothermus taiwanensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A059VAZ3 (Residues: 1-793; Coverage: 100%)
Gene names: Mcate_02015, lon, lon1_1, lonA1
Sequence domains:
Lon protease Chain: F
Molecule details ›
Chain: F
Length: 570 amino acids
Theoretical weight: 63.19 KDa
Source organism: Meiothermus taiwanensis
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: A0A059VAZ3 (Residues: 242-793; Coverage: 70%)
Gene names: Mcate_02015, lon, lon1_1, lonA1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 4 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 4.42Å
Relevant EMDB volumes: EMD-36867
Expression system: Escherichia coli BL21(DE3)

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