› 1lv0

X-ray diffraction
2Å resolution

Crystal structure of the Rab effector guanine nucleotide dissociation inhibitor (GDI) in complex with a geranylgeranyl (GG) peptide

Released:
DOI: 10.2210/pdb1lv0/pdb
PDB entry 1lv0 coloured by chain, front view.
PDB entry 1lv0 coloured by chain, side view.
PDB entry 1lv0 coloured by chain, top view.
Source organism: Bos taurus
Primary publication:
Geranylgeranyl switching regulates GDI-Rab GTPase recycling.
An Y, Shao Y, Alory C, Matteson J, Sakisaka T, Chen W, Gibbs RA, Wilson IA, Balch WE
Structure 11 347-57 (2003)
PMID: 12623022

Function and Biology Details

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

Structure analysis Details

Assembly composition:
monomeric (preferred)
Assembly name:
PDBe Complex ID:
PDB-CPX-149445 (preferred)
Entry contents:
1 distinct polypeptide molecule
Macromolecule:
Rab GDP dissociation inhibitor alpha Chain: A
Molecule details ›
Chain: A
Length: 449 amino acids
Theoretical weight: 50.9 KDa
Source organism: Bos taurus
Expression system: Escherichia coli
UniProt:
  • Canonical: P21856 (Residues: 1-447; Coverage: 100%)
Gene names: GDI1, RABGDIA
Sequence domains: GDP dissociation inhibitor
Structure domains:

Ligands and Environments

2 bound ligands:
Ligand SO4 3 x SO4
Ligand GER 1 x GER
No modified residues

Experiments and Validation Details

Entry percentile scores
X-ray source: SSRL BEAMLINE BL9-2
Spacegroup: P21
Unit cell:
a: 62.23Å b: 42.861Å c: 89.104Å
α: 90° β: 103.53° γ: 90°
R-values:
R R work R free
0.196 0.196 0.249
Expression system: Escherichia coli

Quick links

Citations

13 review citations

Role of Rab GTPases in membrane traffic and cell physiology.
Hutagalung et al. (2011)
12 more

3 mentions without citation

Multiple domain insertions and losses in the evolution of the Rab prenylation complex.
Rasteiro et al. (2007)
2 more