› 3ffk

X-ray diffraction
3Å resolution

Crystal structure of human Gelsolin domains G1-G3 bound to Actin

Released:
DOI: 10.2210/pdb3ffk/pdb
PDB entry 3ffk coloured by chain, front view.
PDB entry 3ffk coloured by chain, side view.
PDB entry 3ffk coloured by chain, top view.
Source organisms:
Primary publication:
Ca2+ binding by domain 2 plays a critical role in the activation and stabilization of gelsolin.
Nag S, Ma Q, Wang H, Chumnarnsilpa S, Lee WL, Larsson M, Kannan B, Hernandez-Valladares M, Burtnick LD, Robinson RC
Proc Natl Acad Sci U S A 106 13713-8 (2009)
PMID: 19666512

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139014 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Gelsolin Chains: A, D
Molecule details ›
Chains: A, D
Length: 377 amino acids
Theoretical weight: 41.94 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06396 (Residues: 52-426; Coverage: 50%)
Gene name: GSN
Sequence domains: Gelsolin repeat
Structure domains: Severin
Actin, alpha skeletal muscle Chains: B, E
Molecule details ›
Chains: B, E
Length: 377 amino acids
Theoretical weight: 42.1 KDa
Source organism: Oryctolagus cuniculus
UniProt:
  • Canonical: P68135 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand CA 10 x CA
Ligand ATP 2 x ATP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSRRC BEAMLINE BL13B1
Spacegroup: P212121
Unit cell:
a: 102.179Å b: 146.923Å c: 148.301Å
α: 90° β: 90° γ: 90°
R-values:
R R work R free
0.204 0.201 0.273
Expression system: Escherichia coli

Quick links

Citations

9 review citations

Actin in dendritic spines: connecting dynamics to function.
Hotulainen et al. (2010)
8 more

9 mentions without citation

Gelsolin amyloidosis: genetics, biochemistry, pathology and possible strategies for therapeutic intervention.
Solomon et al. (2012)
8 more