› 1p3i

X-ray diffraction
2.3Å resolution

Crystallographic Studies of Nucleosome Core Particles containing Histone 'Sin' Mutants

Released:
DOI: 10.2210/pdb1p3i/pdb
PDB entry 1p3i coloured by chain, front view.
PDB entry 1p3i coloured by chain, side view.
PDB entry 1p3i coloured by chain, top view.
Source organism: Xenopus laevis
Primary publication:
Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions.
Muthurajan UM, Bao Y, Forsberg LJ, Edayathumangalam RS, Dyer PN, White CL, Luger K
EMBO J 23 260-71 (2004)
PMID: 14739929

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero decamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-506360 (preferred)
Entry contents:
4 distinct polypeptide molecules
1 distinct DNA molecule
Macromolecules (5 distinct):
Histone H3.2 Chains: A, E
Molecule details ›
Chains: A, E
Length: 135 amino acids
Theoretical weight: 15.36 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P84233 (Residues: 2-136; Coverage: 99%)
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Histone H4 Chains: B, F
Molecule details ›
Chains: B, F
Length: 102 amino acids
Theoretical weight: 11.24 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P62799 (Residues: 2-103; Coverage: 99%)
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A
Histone H2A type 1 Chains: C, G
Molecule details ›
Chains: C, G
Length: 129 amino acids
Theoretical weight: 13.96 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P06897 (Residues: 2-130; Coverage: 99%)
Sequence domains:
Structure domains: Histone, subunit A
Histone H2B 1.1 Chains: D, H
Molecule details ›
Chains: D, H
Length: 125 amino acids
Theoretical weight: 13.83 KDa
Source organism: Xenopus laevis
Expression system: Escherichia coli
UniProt:
  • Canonical: P02281 (Residues: 2-126; Coverage: 99%)
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Palindromic 146bp Human Alpha-Satellite DNA fragment Chains: I, J
Molecule details ›
Chains: I, J
Length: 146 nucleotides
Theoretical weight: 45.05 KDa

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P212121
Unit cell:
a: 106.61Å b: 109.752Å c: 182.3Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.242 0.242 0.275
Expression system: Escherichia coli

Quick links

Citations

22 review citations

Regulated nucleosome mobility and the histone code.
Cosgrove et al. (2004)
21 more

9 mentions without citation

Crystal structures of histone Sin mutant nucleosomes reveal altered protein-DNA interactions.
Muthurajan et al. (2004)
8 more