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Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

MPG-Autoren
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Pylypenko,  Olena
Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society;

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Goody,  Roger S.
Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society;

Externe Ressourcen

http://science.sciencemag.org/content/302/5645/646.full-text.pdf+html
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https://dx.doi.org/10.1126/science.1087761
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Zitation

Rak, A., Pylypenko, O., Durek, T., Watzke, A., Kushnir, S., Brunsveld, L., et al. (2003). Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase. Science, 302(5645), 646-650. doi:10.1126/science.1087761.


Zitierlink: https://hdl.handle.net/11858/00-001M-0000-002A-0F2A-7
Zusammenfassung
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.