› 3aa0

X-ray diffraction
1.7Å resolution

Crystal structure of Actin Capping Protein in complex with the Cp-binding motif derived from CARMIL

Released:
DOI: 10.2210/pdb3aa0/pdb
PDB entry 3aa0 coloured by chain, front view.
PDB entry 3aa0 coloured by chain, side view.
PDB entry 3aa0 coloured by chain, top view.
Source organism: Gallus gallus
Primary publication:
Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition.
Takeda S, Minakata S, Koike R, Kawahata I, Narita A, Kitazawa M, Ota M, Yamakuni T, Maéda Y, Nitanai Y
OpenAccess logo PLoS Biol 8 e1000416 (2010)
PMID: 20625546

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero trimer (preferred)
PDBe Complex ID:
PDB-CPX-146480 (preferred)
Entry contents:
3 distinct polypeptide molecules
Macromolecules (3 distinct):
F-actin-capping protein subunit alpha-1 Chain: A
Molecule details ›
Chain: A
Length: 286 amino acids
Theoretical weight: 33 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P13127 (Residues: 1-286; Coverage: 100%)
Gene name: CAPZA1
Sequence domains: F-actin capping protein alpha subunit
Structure domains:
F-actin-capping protein subunit beta isoforms 1 and 2 Chain: B
Molecule details ›
Chain: B
Length: 244 amino acids
Theoretical weight: 27.47 KDa
Source organism: Gallus gallus
Expression system: Escherichia coli
UniProt:
  • Canonical: P14315 (Residues: 1-244; Coverage: 88%)
Gene name: CAPZB
Sequence domains: F-actin capping protein, beta subunit
Structure domains:
F-actin-uncapping protein LRRC16A Chain: C
Molecule details ›
Chain: C
Length: 21 amino acids
Theoretical weight: 2.61 KDa
UniProt:
  • Canonical: Q6EDY6 (Residues: 985-1005; Coverage: 2%)
Gene names: Carmil, Carmil1, Lrrc16, Lrrc16a

Ligands and Environments

1 bound ligand:
Ligand CO3 1 x CO3
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SPRING-8 BEAMLINE BL26B1
Spacegroup: P212121
Unit cell:
a: 54.814Å b: 67.921Å c: 137.086Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.194 0.191 0.239
Expression system: Escherichia coli

Quick links

Citations

12 review citations

Capping protein regulators fine-tune actin assembly dynamics.
Edwards et al. (2014)
11 more

3 mentions without citation

Two distinct mechanisms for actin capping protein regulation--steric and allosteric inhibition.
Takeda et al. (2010)
2 more