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2bcg

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(New page: 200px<br /><applet load="2bcg" size="450" color="white" frame="true" align="right" spinBox="true" caption="2bcg, resolution 1.48&Aring;" /> '''Structure of doubly ...)
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caption="2bcg, resolution 1.48&Aring;" />
'''Structure of doubly prenylated Ypt1:GDI complex'''<br />
'''Structure of doubly prenylated Ypt1:GDI complex'''<br />
==Overview==
==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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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.
==About this Structure==
==About this Structure==
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2BCG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG, GDP, GER and TRS as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2BCG OCA].
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2BCG is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=GDP:'>GDP</scene>, <scene name='pdbligand=GER:'>GER</scene> and <scene name='pdbligand=TRS:'>TRS</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BCG OCA].
==Reference==
==Reference==
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[[Category: vesicular transport]]
[[Category: vesicular transport]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:43:27 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:21 2008''

Revision as of 14:36, 21 February 2008

Image:2bcg.gif

2bcg, resolution 1.48Å

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Structure of doubly prenylated Ypt1:GDI complex

Overview

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.

About this Structure

2BCG is a Protein complex structure of sequences from Saccharomyces cerevisiae with , , and as ligands. 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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