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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.

Pubmed ID: 14576435

Authors

  • Rak A
  • Pylypenko O
  • Durek T
  • Watzke A
  • Kushnir S
  • Brunsveld L
  • Waldmann H
  • Goody RS
  • Alexandrov K

Journal

Science (New York, N.Y.)

Publication Data

October 24, 2003

Associated Grants

None

Mesh Terms

  • Binding Sites
  • Crystallization
  • Crystallography, X-Ray
  • Guanine Nucleotide Dissociation Inhibitors
  • Guanosine Diphosphate
  • Hydrogen Bonding
  • Hydrophobic and Hydrophilic Interactions
  • 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