› 1x0t

X-ray diffraction
1.6Å resolution

Crystal structure of ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3

Released:
DOI: 10.2210/pdb1x0t/pdb
PDB entry 1x0t coloured by chain, front view.
PDB entry 1x0t coloured by chain, side view.
PDB entry 1x0t coloured by chain, top view.
Source organism: Pyrococcus horikoshii OT3
Primary publication:
Crystal structure of a ribonuclease P protein Ph1601p from Pyrococcus horikoshii OT3: an archaeal homologue of human nuclear ribonuclease P protein Rpp21.
Kakuta Y, Ishimatsu I, Numata T, Kimura K, Yao M, Tanaka I, Kimura M
Biochemistry 44 12086-93 (2005)
PMID: 16142906

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 analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-129839 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Ribonuclease P protein component 4 Chain: A
Molecule details ›
Chain: A
Length: 120 amino acids
Theoretical weight: 14.63 KDa
Source organism: Pyrococcus horikoshii OT3
Expression system: Escherichia coli
UniProt:
  • Canonical: O59248 (Residues: 1-120; Coverage: 100%)
Gene names: PH1601, rnp4
Sequence domains: RNAse P Rpr2/Rpp21/SNM1 subunit domain
Structure domains:

Ligands and Environments

1 bound ligand:
Ligand ZN 1 x ZN
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL41XU
Spacegroup: P212121
Unit cell:
a: 42.594Å b: 52.691Å c: 62.672Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.217 0.217 0.245
Expression system: Escherichia coli

Quick links

Citations

7 review citations

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

2 mentions without citation

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