› 7ypk

Electron Microscopy
3.4Å resolution

Close-ring hexamer of the substrate-bound Lon protease with an S678A mutation

Released:
DOI: 10.2210/pdb7ypk/pdb
PDB entry 7ypk coloured by chain, front view.
PDB entry 7ypk coloured by chain, side view.
PDB entry 7ypk coloured by chain, top view.
Source organisms:
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
OpenAccess logo Nat Commun 14 7340 (2023)
PMID: 37957149
Related structures: EMD-34003

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 heptamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-232516 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
alpha-S1-casein Chain: S
Molecule details ›
Chain: S
Length: 19 amino acids
Theoretical weight: 1.64 KDa
Source organism: Bos taurus
Lon protease Chains: A, B, C, D, E, F
Molecule details ›
Chains: A, B, C, D, E, F
Length: 793 amino acids
Theoretical weight: 88.54 KDa
Source organism: Meiothermus taiwanensis
Expression system: Escherichia coli
UniProt:
  • Canonical: A0A059VAZ3 (Residues: 1-793; Coverage: 100%)
Gene names: Mcate_02015, lon, lon1_1, lonA1
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 6 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.4Å
Relevant EMDB volumes: EMD-34003
Expression system: Escherichia coli

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