Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase.
Rab/Ypt guanosine triphosphatases (GTPases) represent a family of key membrane traffic regulators in eukaryotic cells whose function is governed by the guanosine diphosphate (GDP) dissociation inhibitor (RabGDI). Using a combination of chemical synthesis and protein engineering, we generated and crystallized the monoprenylated Ypt1:RabGDI complex. The structure of the complex was ... solved to 1.5 angstrom resolution and provides a structural basis for the ability of RabGDI to inhibit the release of nucleotide by Rab proteins. Isoprenoid binding requires a conformational change that opens a cavity in the hydrophobic core of its domain II. Analysis of the structure provides a molecular basis for understanding a RabGDI mutant that causes mental retardation in humans.
Mesh Terms:
Binding Sites, Crystallization, Crystallography, X-Ray, Guanine Nucleotide Dissociation Inhibitors, Guanosine Diphosphate, Hydrogen Bonding, Hydrophobicity, Lipid Metabolism, Magnesium, Models, Molecular, Mutation, Protein Binding, Protein Conformation, Protein Prenylation, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae Proteins, rab GTP-Binding Proteins
Binding Sites, Crystallization, Crystallography, X-Ray, Guanine Nucleotide Dissociation Inhibitors, Guanosine Diphosphate, Hydrogen Bonding, Hydrophobicity, Lipid Metabolism, Magnesium, Models, Molecular, Mutation, Protein Binding, Protein Conformation, Protein Prenylation, Protein Structure, Secondary, Protein Structure, Tertiary, Recombinant Proteins, Saccharomyces cerevisiae Proteins, rab GTP-Binding Proteins
Science
Date: Oct. 24, 2003
PubMed ID: 14576435
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