7f3e

Electron Microscopy
3.62Å resolution

Cryo-EM structure of the minimal protein-only RNase P from Aquifex aeolicus

Released:

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dodecamer (preferred)
PDBe Complex ID:
PDB-CPX-130414 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
RNA-free ribonuclease P 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: 195 amino acids
Theoretical weight: 22.82 KDa
Source organism: Aquifex aeolicus VF5
Expression system: Escherichia coli
UniProt:
  • Canonical: O67035 (Residues: 1-192; Coverage: 100%)
Gene name: aq_880
Sequence domains: PINc domain ribonuclease

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.62Å
Relevant EMDB volumes: EMD-31432
Expression system: Escherichia coli