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3cph
From Proteopedia
Crystal structure of Sec4 in complex with Rab-GDI
Overview
RabGDI-facilitated extraction of prenylated Rab proteins from membranes plays an important role in vesicular membrane trafficking. The investigated thermodynamic properties of yeast Rab:GDI and Rab:MRS6 complexes demonstrated differences in the Rab binding properties of the closely related RabGDI and MRS6 proteins, consistent with their functional diversity. The importance of the Rab C-terminus and its prenylation for GDI/MRS6 binding was demonstrated using both biochemical and structural data. The presented structures of the apo-form yeast RabGDI and its two complexes with unprenylated Rab proteins, together with the earlier published structures of the prenylated Ypt1:RabGDI provide evidence of allosteric regulation of the GDI lipid binding site opening, which plays a key role in the proposed mechanism of GDI mediated Rab extraction. We suggest a model for the interaction of GDI with prenylated Rab proteins which incorporates a stepwise increase in affinity as the 3 different partial interactions are successively formed.
About this Structure
3CPH is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
Reference
A structural model of the GDI rab membrane extraction mechanism., Ignatev A, Kravchenko S, Rak A, Goody RS, Pylypenko O, J Biol Chem. 2008 Apr 20;. PMID:18426803 Page seeded by OCA on Wed May 7 08:56:42 2008
Categories: Protein complex | Saccharomyces cerevisiae | Goody, R S. | Ignatev, A. | Kravchenko, S. | Pylypenko, O. | Rak, A. | Cytoplasm | Cytoplasmic vesicle | Exocytosis | Gtp-binding | Gtpase activation | Lipoprotein | Membrane | Nucleotide-binding | Palmitate | Phosphoprotein | Prenylation | Protein transport | Rab gtpase | Vesicular transport
