› 1pxy

X-ray diffraction
2.4Å resolution

Crystal structure of the actin-crosslinking core of Arabidopsis fimbrin

Released:
DOI: 10.2210/pdb1pxy/pdb
PDB entry 1pxy coloured by chain, front view.
PDB entry 1pxy coloured by chain, side view.
PDB entry 1pxy coloured by chain, top view.
Source organism: Arabidopsis thaliana
Primary publication:
Structure of the actin crosslinking core of fimbrin.
Klein MG, Shi W, Ramagopal U, Tseng Y, Wirtz D, Kovar DR, Staiger CJ, Almo SC
Structure 12 999-1013 (2004)
PMID: 15274920

Function and Biology Details

Biochemical function:
Biological process:
Cellular component:
  • not assigned
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181506 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Fimbrin-1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 506 amino acids
Theoretical weight: 57.55 KDa
Source organism: Arabidopsis thaliana
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7G188 (Residues: 123-623; Coverage: 73%)
Gene names: At4g26700, F10M23.40, FIM1
Sequence domains: Calponin homology (CH) domain
Structure domains: Calponin-like domain

Ligands and Environments

No bound ligands
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: NSLS BEAMLINE X9B
Spacegroup: P21
Unit cell:
a: 62.688Å b: 104.981Å c: 104.411Å
α: 90° β: 103.93° γ: 90°
R-values:
R R work R free
0.229 0.229 0.27
Expression system: Escherichia coli BL21

Quick links

Citations

16 review citations

Actin dynamics, architecture, and mechanics in cell motility.
Blanchoin et al. (2014)
15 more

4 mentions without citation

Opening of tandem calponin homology domains regulates their affinity for F-actin.
Galkin et al. (2010)
3 more