1UKV

Structure of RabGDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

Summary for 1UKV

• Entry DOI: 10.2210/pdb1ukv/pdb
• Descriptor: Secretory pathway GDP dissociation inhibitor, GTP-binding protein YPT1, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: gtpase, hydrolase, gdp dissociation inhibitor, vesicular transport, protein transport
• Biological source: Saccharomyces cerevisiae (baker's yeast); More
• Cellular location: Cytoplasm: P39958; Endoplasmic reticulum membrane; Peripheral membrane protein: P01123
• Total number of polymer chains: 2
• Total formula weight: 75448.65

Authors

Rak, A.,Pylypenko, O.,Durek, T.,Watzke, A.,Kushnir, S.,Brunsveld, L.,Waldmann, H.,Goody, R.S.,Alexandrov, K. (deposition date: 2003-09-01, release date: 2004-09-01, Last modification date: 2024-10-30)

Primary citation

Rak, A.,Pylypenko, O.,Durek, T.,Watzke, A.,Kushnir, S.,Brunsveld, L.,Waldmann, H.,Goody, R.S.,Alexandrov, K.
Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase
Science, 302:646-650, 2003

PubMed Abstract: 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: 14576435
DOI: 10.1126/science.1087761

Experimental method

X-RAY DIFFRACTION (1.5 Å)