› 2i2q

X-ray diffraction
1.72Å resolution

Fission Yeast cofilin

Released:
DOI: 10.2210/pdb2i2q/pdb
PDB entry 2i2q coloured by chain, front view.
PDB entry 2i2q coloured by chain, side view.
PDB entry 2i2q coloured by chain, top view.
Source organism: Schizosaccharomyces pombe
Primary publication:
Mechanism of actin filament turnover by severing and nucleation at different concentrations of ADF/cofilin.
Andrianantoandro E, Pollard TD
Mol. Cell 24 13-23 (2006)
PMID: 17018289

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160304 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Cofilin Chain: A
Molecule details ›
Chain: A
Length: 137 amino acids
Theoretical weight: 15.64 KDa
Source organism: Schizosaccharomyces pombe
Expression system: Escherichia coli
UniProt:
  • Canonical: P78929 (Residues: 1-137; Coverage: 100%)
Gene names: SPAC20G4.06c, adf1, cof1
Sequence domains: Cofilin/tropomyosin-type actin-binding protein
Structure domains: Severin

Ligands and Environments

3 bound ligands:
Ligand SO4 2 x SO4
Ligand LDA 1 x LDA
Ligand EDO 4 x EDO
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: RIGAKU RU200
Spacegroup: P43212
Unit cell:
a: 81.915Å b: 81.915Å c: 61.863Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.246 0.236 0.256
Expression system: Escherichia coli

Quick links

Citations

110 review citations

Regulation of actin filament assembly by Arp2/3 complex and formins.
Pollard TD. (2007)
109 more

7 mentions without citation

Actin filament severing by cofilin is more important for assembly than constriction of the cytokinetic contractile ring.
Chen et al. (2011)
6 more