3iab

X-ray diffraction
2.7Å resolution

Crystal structure of RNase P /RNase MRP proteins Pop6, Pop7 in a complex with the P3 domain of RNase MRP RNA

Released:

Function and Biology Details

Reaction catalysed:
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Biochemical function:
Cellular component:

Structure analysis Details

Assemblies composition:
hetero trimer (preferred)
hetero hexamer
PDBe Complex ID:
PDB-CPX-153604 (preferred)
Entry contents:
2 distinct polypeptide molecules
1 distinct RNA molecule
Macromolecules (3 distinct):
Ribonucleases P/MRP protein subunit POP6 Chain: A
Molecule details ›
Chain: A
Length: 158 amino acids
Theoretical weight: 18.44 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P53218 (Residues: 1-158; Coverage: 100%)
Gene names: POP6, YGR030C
Sequence domains: Alba
Ribonucleases P/MRP protein subunit POP7 Chain: B
Molecule details ›
Chain: B
Length: 140 amino acids
Theoretical weight: 15.98 KDa
Source organism: Saccharomyces cerevisiae
Expression system: Escherichia coli
UniProt:
  • Canonical: P38291 (Residues: 1-140; Coverage: 100%)
Gene names: POP7, RPP2, YBR1219, YBR167C
Sequence domains: Rpp20 subunit of nuclear RNase MRP and P
Structure domains: Alba-like domain
P3 domain of the RNA component of RNase MRP Chain: R
Molecule details ›
Chain: R
Length: 46 nucleotides
Theoretical weight: 14.83 KDa

Ligands and Environments

1 bound ligand:
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X29A
Spacegroup: P4222
Unit cell:
a: 126.514Å b: 126.514Å c: 76.766Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.25 0.265
Expression system: Escherichia coli