› 7ccc

X-ray diffraction
3.2Å resolution

The structure of the actin filament uncapping complex mediated by twinfilin

Released:
DOI: 10.2210/pdb7ccc/pdb
PDB entry 7ccc coloured by chain, front view.
PDB entry 7ccc coloured by chain, side view.
PDB entry 7ccc coloured by chain, top view.
Source organisms:
Primary publication:
The structure of the actin filament uncapping complex mediated by twinfilin.
Mwangangi DM, Manser E, Robinson RC
Sci Adv 7 (2021)
PMID: 33571120

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-155649 (preferred)
Entry contents:
4 distinct polypeptide molecules
Macromolecules (4 distinct):
Actin, alpha skeletal muscle Chains: A, E
Molecule details ›
Chains: A, E
Length: 377 amino acids
Theoretical weight: 42.11 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Twinfilin-1 Chain: B
Molecule details ›
Chain: B
Length: 350 amino acids
Theoretical weight: 40.34 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: Q12792 (Residues: 1-350; Coverage: 100%)
Gene names: PTK9, TWF1
Sequence domains: Cofilin/tropomyosin-type actin-binding protein
F-actin-capping protein subunit alpha-1 Chain: C
Molecule details ›
Chain: C
Length: 286 amino acids
Theoretical weight: 32.98 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: P47753 (Residues: 1-286; Coverage: 100%)
Gene names: Cappa1, Capza1
Sequence domains: F-actin capping protein alpha subunit
F-actin-capping protein subunit beta Chain: D
Molecule details ›
Chain: D
Length: 272 amino acids
Theoretical weight: 30.67 KDa
Source organism: Mus musculus
Expression system: Escherichia coli
UniProt:
  • Canonical: Q923G3 (Residues: 1-272; Coverage: 100%)
Gene name: Capzb
Sequence domains: F-actin capping protein, beta subunit

Ligands and Environments

2 bound ligands:
Ligand CA 2 x CA
Ligand ADP 2 x ADP
1 modified residue:
Ligand HIC 2 x HIC

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE TPS 05A
Spacegroup: P212121
Unit cell:
a: 74.759Å b: 168.662Å c: 176.989Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.192 0.186 0.238
Expression system: Escherichia coli

Quick links

Citations

4 review citations

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

1 mention without citation

Computational study of the impact of nucleotide variations on highly conserved proteins: In the case of actin.
Duong et al. (2022)