› 5ooe

Electron Microscopy
3.6Å resolution

Cryo-EM structure of F-actin in complex with AppNHp (AMPPNP)

Released:
DOI: 10.2210/pdb5ooe/pdb
PDB entry 5ooe coloured by chain, front view.
PDB entry 5ooe coloured by chain, side view.
PDB entry 5ooe coloured by chain, top view.
Source organism: Oryctolagus cuniculus
Primary publication:
Structural transitions of F-actin upon ATP hydrolysis at near-atomic resolution revealed by cryo-EM.
Merino F, Pospich S, Funk J, Wagner T, Küllmer F, Arndt HD, Bieling P, Raunser S
Nat Struct Mol Biol 25 528-537 (2018)
PMID: 29867215
Related structures: EMD-3838

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo pentamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-159326 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Actin, alpha skeletal muscle Chains: A, B, C, D, E
Molecule details ›
Chains: A, B, C, D, E
Length: 375 amino acids
Theoretical weight: 41.88 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 3-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin

Ligands and Environments

2 bound ligands:
Ligand ANP 5 x ANP
Ligand MG 5 x MG
1 modified residue:
Ligand HIC 5 x HIC

Experiments and Validation Details

Entry percentile scores
Resolution: 3.6Å
Relevant EMDB volumes: EMD-3838

Quick links

Citations

8 review citations

Biochemical and mechanical regulation of actin dynamics.
Lappalainen et al. (2022)
7 more

4 mentions without citation

Towards a structural understanding of the remodeling of the actin cytoskeleton.
Merino et al. (2020)
3 more