2BCG
Structure of doubly prenylated Ypt1:GDI complex
Summary for 2BCG
| Entry DOI | 10.2210/pdb2bcg/pdb |
| Related | 1ukv |
| Descriptor | Secretory pathway GDP dissociation inhibitor, GTP-binding protein YPT1, GERAN-8-YL GERAN, ... (7 entities in total) |
| Functional Keywords | rabgtpase, geranylgeranylation, 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 | 75891.36 |
| Authors | Pylypenko, O.,Rak, A.,Alexandrov, K. (deposition date: 2005-10-19, release date: 2006-01-17, Last modification date: 2023-08-23) |
| Primary citation | Pylypenko, O.,Rak, A.,Durek, T.,Kushnir, S.,Dursina, B.E.,Thomae, N.H.,Constantinescu, A.T.,Brunsveld, L.,Watzke, A.,Waldmann, H.,Goody, R.S.,Alexandrov, K. Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-mediated Rab recycling Embo J., 25:13-23, 2006 Cited by PubMed Abstract: In eukaryotic cells Rab/Ypt GTPases represent a family of key membrane traffic controllers that associate with their targeted membranes via C-terminally conjugated geranylgeranyl groups. GDP dissociation inhibitor (GDI) is a general and essential regulator of Rab recycling that extracts prenylated Rab proteins from membranes at the end of their cycle of activity and facilitates their delivery to the donor membranes. Here, we present the structure of a complex between GDI and a doubly prenylated Rab protein. We show that one geranylgeranyl residue is deeply buried in a hydrophobic pocket formed by domain II of GDI, whereas the other lipid is more exposed to solvent and is skewed across several atoms of the first moiety. Based on structural information and biophysical measurements, we propose mechanistic and thermodynamic models for GDI and Rab escort protein-mediated interaction of RabGTPase with intracellular membranes. PubMed: 16395334DOI: 10.1038/sj.emboj.7600921 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (1.48 Å) |
Structure validation
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