3cph | pdb_00003cph
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
Proteopedia Page Contributors and Editors (what is this?)
- Pages with broken file links
- 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
