1LV0

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

Summary for 1LV0

• Entry DOI: 10.2210/pdb1lv0/pdb
• Related: 1D5T 1GND
• Descriptor: RAB GDP disossociation inhibitor alpha, SULFATE ION, GERAN-8-YL GERAN, ... (4 entities in total)
• Functional Keywords: protein-ligand complex, signaling protein
• Biological source: Bos taurus (cattle)
• Cellular location: Cytoplasm (By similarity): P21856
• Total number of polymer chains: 1
• Total formula weight: 51459.43

Authors

An, Y.,Shao, Y.,Alory, C.,Matteson, J.,Sakisaka, T.,Chen, W.,Gibbs, R.A.,Wilson, I.A.,Balch, W.E. (deposition date: 2002-05-23, release date: 2003-08-05, Last modification date: 2024-02-14)

Primary citation

An, Y.,Shao, Y.,Alory, C.,Matteson, J.,Sakisaka, T.,Chen, W.,Gibbs, R.A.,Wilson, I.A.,Balch, W.E.
Geranylgeranyl switching regulates GDI-Rab GTPase recycling.
Structure, 11:347-357, 2003

PubMed Abstract: Rab GTPases, key regulators of membrane targeting and fusion, require the covalent attachment of geranylgeranyl lipids to their C terminus for function. To elucidate the role of lipid in Rab recycling, we have determined the crystal structure of Rab guanine nucleotide dissociation inhibitor (alphaGDI) in complex with a geranylgeranyl (GG) ligand (H(2)N-Cys-(S-GG)-OMe). The lipid is bound beneath the Rab binding platform in a shallow hydrophobic groove. Mutation of the binding pocket in the brain-specific alphaGDI leads to mental retardation. Strikingly, lipid binding acts through a conserved allosteric switching mechanism to promote release of the GDI-Rab[GDP] complex from the membrane.

PubMed: 12623022
DOI: 10.1016/S0969-2126(03)00034-0

Experimental method

X-RAY DIFFRACTION (2 Å)