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2bcg

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{{STRUCTURE_2bcg| PDB=2bcg | SCENE= }}
{{STRUCTURE_2bcg| PDB=2bcg | SCENE= }}
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'''Structure of doubly prenylated Ypt1:GDI complex'''
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===Structure of doubly prenylated Ypt1:GDI complex===
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==Overview==
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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.
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{{ABSTRACT_PUBMED_16395334}}
==About this Structure==
==About this Structure==
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[[Category: Rabgtpase]]
[[Category: Rabgtpase]]
[[Category: Vesicular transport]]
[[Category: Vesicular transport]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:53:08 2008''

Revision as of 11:53, 28 July 2008

Image:2bcg.png

Template:STRUCTURE 2bcg

Structure of doubly prenylated Ypt1:GDI complex

Template:ABSTRACT PUBMED 16395334

About this Structure

2BCG is a Protein complex structure of sequences from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structure of doubly prenylated Ypt1:GDI complex and the mechanism of GDI-mediated Rab recycling., Pylypenko O, Rak A, Durek T, Kushnir S, Dursina BE, Thomae NH, Constantinescu AT, Brunsveld L, Watzke A, Waldmann H, Goody RS, Alexandrov K, EMBO J. 2006 Jan 11;25(1):13-23. Epub 2006 Jan 5. PMID:16395334

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