› 1mdu

X-ray diffraction
2.2Å resolution

Crystal structure of the chicken actin trimer complexed with human gelsolin segment 1 (GS-1)

Released:
DOI: 10.2210/pdb1mdu/pdb
PDB entry 1mdu coloured by chain, front view.
PDB entry 1mdu coloured by chain, side view.
PDB entry 1mdu coloured by chain, top view.
Source organisms:
Primary publication:
Structure of an F-actin trimer disrupted by gelsolin and implications for the mechanism of severing.
Dawson JF, Sablin EP, Spudich JA, Fletterick RJ
J Biol Chem 278 1229-38 (2003)
PMID: 12356759

Function and Biology Details

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

Structure analysis Details

Assembly composition:
hetero hexamer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-139023 (preferred)
Entry contents:
2 distinct polypeptide molecules
Macromolecules (2 distinct):
Gelsolin Chains: A, D
Molecule details ›
Chains: A, D
Length: 125 amino acids
Theoretical weight: 14.07 KDa
Source organism: Homo sapiens
Expression system: Escherichia coli
UniProt:
  • Canonical: P06396 (Residues: 52-176; Coverage: 17%)
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: 42.11 KDa
Source organism: Gallus gallus
UniProt:
  • Canonical: P68139 (Residues: 1-377; Coverage: 100%)
Gene names: ACTA, ACTA1
Sequence domains: Actin
Structure domains:

Ligands and Environments

3 bound ligands:
Ligand CA 7 x CA
Ligand TRS 1 x TRS
Ligand ATP 2 x ATP
1 modified residue:
Ligand HIC 2 x HIC

Experiments and Validation Details

Entry percentile scores
X-ray source: ALS BEAMLINE 5.0.2
Spacegroup: P21
Unit cell:
a: 67.187Å b: 75.942Å c: 96.747Å
α: 90° β: 91.87° γ: 90°
R-values:
R R work R free
0.207 0.193 0.233
Expression system: Escherichia coli

Quick links

Citations

2 review citations

The gelsolin family of actin regulatory proteins: modular structures, versatile functions.
McGough et al. (2003)
1 more

5 mentions without citation

Identification of transient hub proteins and the possible structural basis for their multiple interactions.
Higurashi et al. (2008)
4 more