› 5i9e

X-ray diffraction
2.8Å resolution

Crystal structure of a nuclear actin ternary complex

Released:
DOI: 10.2210/pdb5i9e/pdb
PDB entry 5i9e coloured by chain, front view.
PDB entry 5i9e coloured by chain, side view.
PDB entry 5i9e coloured by chain, top view.
Source organisms:
Primary publication:
Crystal structure of a nuclear actin ternary complex.
Cao T, Sun L, Jiang Y, Huang S, Wang J, Chen Z
Proc Natl Acad Sci U S A 113 8985-90 (2016)
PMID: 27457955

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 trimer (preferred)
PDBe Complex ID:
PDB-CPX-157948 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
Actin-related protein 4 Chains: A, C
Molecule details ›
Chains: A, C
Length: 490 amino acids
Theoretical weight: 54.99 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P80428 (Residues: 1-489; Coverage: 100%)
Gene names: ACT3, ARP4, J1012, YJL081C
Sequence domains: Actin
Structure domains:
Actin Chains: B, D
Molecule details ›
Chains: B, D
Length: 375 amino acids
Theoretical weight: 41.74 KDa
Source organism: Saccharomyces bayanus
Expression system: Spodoptera frugiperda
UniProt:
  • Canonical: P60011 (Residues: 1-375; Coverage: 100%)
Gene name: ACT1
Sequence domains: Actin
Structure domains:
Helicase SWR1 Chains: E, H
Molecule details ›
Chains: E, H
Length: 77 amino acids
Theoretical weight: 9.22 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Escherichia coli
UniProt:
  • Canonical: Q05471 (Residues: 340-410; Coverage: 5%)
Gene names: D9651.6, SWR1, YDR334W
Sequence domains: HSA domain

Ligands and Environments

2 bound ligands:
Ligand MG 4 x MG
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRF BEAMLINE BL17U
Spacegroup: P21212
Unit cell:
a: 110.26Å b: 202.22Å c: 87.01Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.234 0.232 0.284
Expression systems:
  • Spodoptera frugiperda
  • Escherichia coli

Quick links

Citations

11 review citations

Mechanisms of action and regulation of ATP-dependent chromatin-remodelling complexes.
Clapier et al. (2017)
10 more

6 mentions without citation

Architecture of the Saccharomyces cerevisiae NuA4/TIP60 complex.
Wang et al. (2018)
5 more