› 1o3y

X-ray diffraction
1.5Å resolution

Crystal structure of mouse ARF1 (delta17-Q71L), GTP form

Released:
DOI: 10.2210/pdb1o3y/pdb
PDB entry 1o3y coloured by chain, front view.
PDB entry 1o3y coloured by chain, side view.
PDB entry 1o3y coloured by chain, top view.
Source organism: Mus musculus
Primary publication:
Molecular mechanism of membrane recruitment of GGA by ARF in lysosomal protein transport.
Shiba T, Kawasaki M, Takatsu H, Nogi T, Matsugaki N, Igarashi N, Suzuki M, Kato R, Nakayama K, Wakatsuki S
Nat Struct Biol 10 386-93 (2003)
PMID: 12679809

Function and Biology Details

Reaction catalysed: 
GTP + H(2)O = GDP + phosphate
Biochemical function:
Biological process:
Cellular component:
Sequence domains:
Structure domain:

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-160799 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
ADP-ribosylation factor 1 Chains: A, B
Molecule details ›
Chains: A, B
Length: 166 amino acids
Theoretical weight: 18.95 KDa
Source organism: Mus musculus
Expression system: Escherichia coli BL21
UniProt:
  • Canonical: P84078 (Residues: 18-181; Coverage: 91%)
Gene name: Arf1
Sequence domains: ADP-ribosylation factor family
Structure domains: P-loop containing nucleotide triphosphate hydrolases

Ligands and Environments

2 bound ligands:
Ligand MG 2 x MG
Ligand GTP 2 x GTP
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: PHOTON FACTORY BEAMLINE BL-6A
Spacegroup: C2
Unit cell:
a: 127.605Å b: 50.77Å c: 52.081Å
α: 90° β: 113.37° γ: 90°
R-values:
R R work R free
0.191 0.19 0.211
Expression system: Escherichia coli BL21

Quick links

Citations

21 review citations

ARF proteins: roles in membrane traffic and beyond.
D'Souza-Schorey et al. (2006)
20 more

23 mentions without citation

Conserved functions of membrane active GTPases in coated vesicle formation.
Pucadyil et al. (2009)
22 more