› 5c3i

X-ray diffraction
3.5Å resolution

Crystal structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2

Released:
DOI: 10.2210/pdb5c3i/pdb
PDB entry 5c3i coloured by chain, front view.
PDB entry 5c3i coloured by chain, side view.
PDB entry 5c3i coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
Structure of the quaternary complex of histone H3-H4 heterodimer with chaperone ASF1 and the replicative helicase subunit MCM2.
Wang H, Wang M, Yang N, Xu RM
Protein Cell 6 693-7 (2015)
PMID: 26186914

Function and Biology Details

Reaction catalysed: 
ATP + H(2)O = ADP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-155997 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Histone chaperone ASF1A Chains: A, E, I, M, Q, U
Molecule details ›
Chains: A, E, I, M, Q, U
Length: 188 amino acids
Theoretical weight: 21.38 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: Q9Y294 (Residues: 1-175; Coverage: 86%)
Gene names: ASF1A, CGI-98, HSPC146
Sequence domains: ASF1 like histone chaperone
Structure domains: Histone chaperone ASF1-like
Histone H3.1 Chains: B, F, J, N, R, V
Molecule details ›
Chains: B, F, J, N, R, V
Length: 136 amino acids
Theoretical weight: 15.44 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P68431 (Residues: 1-136; Coverage: 100%)
Gene names: H3C1, H3C10, H3C11, H3C12, H3C2, H3C3, H3C4, H3C6, H3C7, H3C8, H3FA, H3FB, H3FC HIST1H3C, H3FD, H3FF, H3FH, H3FI, H3FJ, H3FK, H3FL, HIST1H3A, HIST1H3B, HIST1H3D, HIST1H3E, HIST1H3F, HIST1H3G, HIST1H3H, HIST1H3I, HIST1H3J
Sequence domains: Core histone H2A/H2B/H3/H4
Structure domains: Histone, subunit A
Histone H4 Chains: C, G, K, O, S, W
Molecule details ›
Chains: C, G, K, O, S, W
Length: 103 amino acids
Theoretical weight: 11.39 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P62805 (Residues: 1-103; Coverage: 100%)
Gene names: H4-16, H4/A, H4/B, H4/C, H4/D, H4/E, H4/G, H4/H, H4/I, H4/J, H4/K, H4/M, H4/N, H4/O, H4C1, H4C11, H4C12, H4C13, H4C14, H4C15, H4C16, H4C2, H4C3, H4C4, H4C5, H4C6, H4C8, H4C9, H4F2, H4FA, H4FB, H4FC, H4FD, H4FE, H4FG, H4FH, H4FI, H4FJ, H4FK, H4FM, H4FN, H4FO, HIST1H4A, HIST1H4B, HIST1H4C, HIST1H4D, HIST1H4E, HIST1H4F, HIST1H4H, HIST1H4I, HIST1H4J, HIST1H4K, HIST1H4L, HIST2H4, HIST2H4A, HIST2H4B, HIST4H4
Sequence domains: Centromere kinetochore component CENP-T histone fold
Structure domains: Histone, subunit A
DNA replication licensing factor MCM2 Chains: D, H, L, P, T, X
Molecule details ›
Chains: D, H, L, P, T, X
Length: 93 amino acids
Theoretical weight: 9.75 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli BL21(DE3)
UniProt:
  • Canonical: P49736 (Residues: 63-124; Coverage: 7%)
Gene names: BM28, CCNL1, CDCL1, KIAA0030, MCM2
Sequence domains: Mini-chromosome maintenance protein 2

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P3121
Unit cell:
a: 147.704Å b: 147.704Å c: 261.796Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.218 0.216 0.253
Expression systems:
  • Escherichia coli BL21(DE3)
  • Escherichia coli

Quick links

Citations

12 review citations

Histone chaperone networks shaping chromatin function.
Hammond et al. (2017)
11 more

5 mentions without citation

Fly Fishing for Histones: Catch and Release by Histone Chaperone Intrinsically Disordered Regions and Acidic Stretches.
Warren et al. (2017)
4 more