› 1uru

X-ray diffraction
2.6Å resolution

Amphiphysin BAR domain from Drosophila

Released:
DOI: 10.2210/pdb1uru/pdb
PDB entry 1uru coloured by chain, front view.
PDB entry 1uru coloured by chain, side view.
PDB entry 1uru coloured by chain, top view.
Source organism: Drosophila melanogaster
Primary publication:
BAR domains as sensors of membrane curvature: the amphiphysin BAR structure.
Peter BJ, Kent HM, Mills IG, Vallis Y, Butler PJ, Evans PR, McMahon HT
Science 303 495-9 (2004)
PMID: 14645856

Function and Biology Details

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

Structure analysis Details

Assembly composition:
homo dimer (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-181589 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Amphiphysin, isoform A Chain: A
Molecule details ›
Chain: A
Length: 244 amino acids
Theoretical weight: 28.27 KDa
Source organism: Drosophila melanogaster
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: Q7KLE5 (Residues: 1-244; Coverage: 41%)
Gene names: Amp, Amph, CG8604, DAMP, Damp, Dmel\CG8604, Dmel_CG8604, amph, dAmp, dAmph, damph
Sequence domains: BAR domain
Structure domains: Arfaptin homology (AH) domain/BAR domain

Ligands and Environments

No bound ligands
1 modified residue:
Ligand MSE 4 x MSE

Experiments and Validation Details

Entry percentile scores
X-ray source: ESRF BEAMLINE ID29
Spacegroup: P3121
Unit cell:
a: 49.586Å b: 49.586Å c: 190.319Å
α: 90° β: 90° γ: 120°
R-values:
R R work R free
0.234 0.236 0.306
Expression system: Escherichia coli BL21

Quick links

Citations

288 review citations

Mechanisms of endocytosis.
Doherty et al. (2009)
287 more

31 mentions without citation

The BAR domain proteins: molding membranes in fission, fusion, and phagy.
Ren et al. (2006)
30 more