2it2

X-ray diffraction
1.5Å resolution

Structure of PH1069 protein from Pyrococcus horikoshii

Released:
Source organism: Pyrococcus horikoshii
Entry authors: Lokanath NK, RIKEN Structural Genomics/Proteomics Initiative (RSGI)

Function and Biology Details

Reaction catalysed:
S-adenosyl-L-methionine + 7-((3S)-(3-amino-3-carboxypropyl))-4-demethylwyosine(37) in tRNA(Phe) = S-adenosyl-L-homocysteine + 7-((3S)-(3-amino-3-carboxypropyl))wyosine(37) in tRNA(Phe)
Biochemical function:
Biological process:
Cellular component:
  • not assigned

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
tRNA(Phe) 7-((3-amino-3-carboxypropyl)-4-demethylwyosine(37)-N(4))-methyltransferase 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 200 amino acids
Theoretical weight: 23.54 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli
UniProt:
  • Canonical: O58796 (Residues: 1-196; Coverage: 100%)
Gene names: PH1069, taw3-1
Sequence domains: Methyltransferase TYW3
Structure domains: tRNA wybutosine-synthesizing-like

Ligands and Environments

No bound ligands
1 modified residue:

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P1
Unit cell:
a: 37.428Å b: 53.902Å c: 53.212Å
α: 104.6° β: 102.9° γ: 109.3°
R-values:
R R work R free
0.25 0.25 0.265
Expression system: Escherichia coli