› 7ksl

Electron Microscopy
3.5Å resolution

Substrate-free human mitochondrial LONP1

Released:
DOI: 10.2210/pdb7ksl/pdb
PDB entry 7ksl coloured by chain, front view.
PDB entry 7ksl coloured by chain, side view.
PDB entry 7ksl coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structures of the human LONP1 protease reveal regulatory steps involved in protease activation.
Shin M, Watson ER, Song AS, Mindrebo JT, Novick SJ, Griffin PR, Wiseman RL, Lander GC
Nat Commun 12 3239 (2021)
PMID: 34050165
Related structures: EMD-23019

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 pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-153221 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Lon protease homolog, mitochondrial Chains: A, B, C, E, F
Molecule details ›
Chains: A, B, C, E, F
Length: 527 amino acids
Theoretical weight: 58.5 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P36776 (Residues: 421-947; Coverage: 55%)
Gene names: LONP1, PRSS15
Sequence domains:

Ligands and Environments

1 bound ligand:
Ligand ADP 5 x ADP
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.5Å
Relevant EMDB volumes: EMD-23019
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

5 review citations

AAA+ proteases: the first line of defense against mitochondrial damage.
Pareek G. (2022)
4 more

2 mentions without citation

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