› 8a5a

Electron Microscopy
3.3Å resolution

Structure of Arp4-Ies4-N-actin-Arp8-Ino80HSA subcomplex (A-module) of INO80

Released:
DOI: 10.2210/pdb8a5a/pdb
PDB entry 8a5a coloured by chain, front view.
PDB entry 8a5a coloured by chain, side view.
PDB entry 8a5a coloured by chain, top view.
Source organism: Saccharomyces cerevisiae S288C
Primary publication:
Structural mechanism of extranucleosomal DNA readout by the INO80 complex.
Kunert F, Metzner FJ, Jung J, Höpfler M, Woike S, Schall K, Kostrewa D, Moldt M, Chen JX, Bantele S, Pfander B, Eustermann S, Hopfner KP
OpenAccess logo Sci Adv 8 eadd3189 (2022)
PMID: 36490333
Related structures: EMD-15163

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero pentamer (preferred)
PDBe Complex ID:
PDB-CPX-273869 (preferred)
Entry contents:
5 distinct polypeptide molecules
Macromolecules (5 distinct):
Chromatin-remodeling ATPase INO80 Chain: G
Molecule details ›
Chain: G
Length: 616 amino acids
Theoretical weight: 72.17 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Trichoplusia ni
UniProt:
  • Canonical: P53115 (Residues: 1-598; Coverage: 40%)
Gene names: G1880, INO80, YGL150C
Sequence domains: DNA-binding domain
Actin-like protein ARP8 Chain: U
Molecule details ›
Chain: U
Length: 881 amino acids
Theoretical weight: 100.32 KDa
Source organism: Saccharomyces cerevisiae S288C
Expression system: Trichoplusia ni
UniProt:
  • Canonical: Q12386 (Residues: 1-881; Coverage: 100%)
Gene names: ARP8, YOR141C, YOR3348C
Sequence domains: Actin
Actin Chain: V
Actin-related protein 4 Chain: W
Ino eighty subunit 4 Chain: X

Ligands and Environments

2 bound ligands:
Ligand ATP 3 x ATP
Ligand MG 3 x MG
No modified residues

Experiments and Validation Details

Entry percentile scores
Resolution: 3.3Å
Relevant EMDB volumes: EMD-15163
Expression system: Trichoplusia ni

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Citations

1 review citation

Energy-driven genome regulation by ATP-dependent chromatin remodellers.
Eustermann et al. (2024)
7 other articles