› 1tsf

X-ray diffraction
1.7Å resolution

Crystal Structure of the Archaeal homolog of Human RNase P Protein Rpp29 from Archaeoglobus fulgidus

Released:
DOI: 10.2210/pdb1tsf/pdb
PDB entry 1tsf coloured by chain, front view.
PDB entry 1tsf coloured by chain, side view.
PDB entry 1tsf coloured by chain, top view.
Source organism: Archaeoglobus fulgidus
Primary publication:
Crystal structure of archaeal ribonuclease P protein aRpp29 from Archaeoglobus fulgidus.
Sidote DJ, Heideker J, Hoffman DW
Biochemistry 43 14128-38 (2004)
PMID: 15518563

Function and Biology Details

Reaction catalysed: 
Endonucleolytic cleavage of RNA, removing 5'-extranucleotides from tRNA precursor.
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-128016 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease P protein component 1 Chain: A
Molecule details ›
Chain: A
Length: 102 amino acids
Theoretical weight: 11.83 KDa
Source organism: Archaeoglobus fulgidus
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O28362 (Residues: 1-102; Coverage: 100%)
Gene names: AF_1917, rnp1
Sequence domains: Ribonuclease P/MRP, subunit p29
Structure domains: Ribonuclease P/MRP, subunit p29

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU300
Spacegroup: P212121
Unit cell:
a: 39.565Å b: 43.79Å c: 49.235Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.25 0.25 0.283
Expression system: Escherichia coli BL21(DE3)

Quick links

Citations

8 review citations

RNase P: interface of the RNA and protein worlds.
Evans et al. (2006)
7 more

1 mention without citation

Of proteins and RNA: the RNase P/MRP family.
Esakova et al. (2010)