› 1ku5

X-ray diffraction
2.3Å resolution

Crystal Structure of recombinant histone HPhA from hyperthermophilic archaeon Pyrococcus horikoshii OT3

Released:
DOI: 10.2210/pdb1ku5/pdb
PDB entry 1ku5 coloured by chain, front view.
PDB entry 1ku5 coloured by chain, side view.
PDB entry 1ku5 coloured by chain, top view.
Source organism: Pyrococcus horikoshii
Primary publication:
Structure based hyperthermostability of archaeal histone HPhA from Pyrococcus horikoshii.
Li T, Sun F, Ji X, Feng Y, Rao Z
J Mol Biol 325 1031-7 (2003)
PMID: 12527306

Function and Biology Details

Biochemical function:
Biological process:
  • not assigned
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-130772 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Archaeal histone A Chains: A, B
Molecule details ›
Chains: A, B
Length: 70 amino acids
Theoretical weight: 7.88 KDa
Source organism: Pyrococcus horikoshii
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: O74098 (Residues: 1-67; Coverage: 100%)
Gene names: PH1782.1, PHS051
Sequence domains: Histone-like transcription factor (CBF/NF-Y) and archaeal histone
Structure domains: Histone, subunit A

Ligands and Environments

2 bound ligands:
Ligand ACT 3 x ACT
Ligand SO4 1 x SO4
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RUH3R
Spacegroup: P21
Unit cell:
a: 34.993Å b: 46.887Å c: 35.023Å
α: 90° β: 103.94° γ: 90°
R-values:
R R work R free
0.216 0.216 0.267
Expression system: Escherichia coli BL21(DE3)

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Citations

2 review citations

Metabolic integration during the evolutionary origin of mitochondria.
Searcy DG. (2003)
1 more