› 7v1m

X-ray diffraction
2.83Å resolution

Structural basis for the co-chaperone relationship of sNASP and ASF1b

Released:
DOI: 10.2210/pdb7v1m/pdb
Model geometry
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PDB entry 7v1m coloured by chain, front view.
PDB entry 7v1m coloured by chain, side view.
PDB entry 7v1m coloured by chain, top view.
Source organism: Homo sapiens
Primary publication:
NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.
Bao H, Carraro M, Flury V, Liu Y, Luo M, Chen L, Groth A, Huang H
OpenAccess logo Nucleic Acids Res 50 5349-5368 (2022)
PMID: 35489058

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
Sequence domains:

Structure analysis Details

Assembly composition:
hetero tetramer (preferred)
PDBe Complex ID:
PDB-CPX-155918 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Histone H3.3 Chains: A, B
Molecule details ›
Chains: A, B
Length: 135 amino acids
Theoretical weight: 15.23 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P84243 (Residues: 2-136; Coverage: 99%)
Gene names: H3-3A, H3-3B, H3.3A, H3.3B, H3F3, H3F3A, H3F3B, PP781
Sequence domains: Core histone H2A/H2B/H3/H4
Histone H4 Chains: C, E
Molecule details ›
Chains: C, E
Length: 102 amino acids
Theoretical weight: 11.26 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'
UniProt:
  • Canonical: P62805 (Residues: 2-103; Coverage: 99%)
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
Histone chaperone ASF1B Chains: D, F
Nuclear autoantigenic sperm protein Chains: G, H

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

wwPDB Validation report is not available for this entry.
X-ray source: SSRF BEAMLINE BL19U1
Spacegroup: P1
Unit cell:
a: 71.951Å b: 71.896Å c: 93.427Å
α: 70.67° β: 70.64° γ: 83.61°
R-values:
R R work R free
0.21 0.202 0.24
Expression system: Escherichia coli 'BL21-Gold(DE3)pLysS AG'

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Citations

1 review citation

Histone 3.3-related chromatinopathy: missense variants throughout H3-3A and H3-3B cause a range of functional consequences across species.
Bryant et al. (2023)
10 other articles

1 mention without citation

NASP maintains histone H3-H4 homeostasis through two distinct H3 binding modes.
Bao et al. (2022)

PDB-REDO

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