4xgl

X-ray diffraction
1.8Å resolution

Structure of the nuclease subunit of human mitochondrial RNase P (MRPP3) at 1.8A

Released:
Source organism: Homo sapiens
Primary publication:
Structure of the nuclease subunit of human mitochondrial RNase P.
Nucleic Acids Res 43 5664-72 (2015)
PMID: 25953853

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
PDBe Complex ID:
PDB-CPX-127287 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Mitochondrial ribonuclease P catalytic subunit Chain: A
Molecule details ›
Chain: A
Length: 379 amino acids
Theoretical weight: 44.12 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli KRX
UniProt:
  • Canonical: O15091 (Residues: 207-583; Coverage: 65%)
Gene names: KIAA0391, MRPP3, PRORP
Sequence domains: Protein-only RNase P

Ligands and Environments

2 bound ligands:
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P43
Unit cell:
a: 99.25Å b: 99.25Å c: 50.94Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.19 0.188 0.228
Expression system: Escherichia coli KRX