1g17
From Proteopedia
(New page: 200px<br /><applet load="1g17" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g17, resolution 2.00Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1g17.gif|left|200px]]<br /><applet load="1g17" size=" | + | [[Image:1g17.gif|left|200px]]<br /><applet load="1g17" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1g17, resolution 2.00Å" /> | caption="1g17, resolution 2.00Å" /> | ||
'''CRYSTAL STRUCTURE OF SEC4-GUANOSINE-5'-(BETA,GAMMA)-IMIDOTRIPHOSPHATE'''<br /> | '''CRYSTAL STRUCTURE OF SEC4-GUANOSINE-5'-(BETA,GAMMA)-IMIDOTRIPHOSPHATE'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We have determined crystal structures of Sec4, a member of the Rab family | + | We have determined crystal structures of Sec4, a member of the Rab family in the G protein superfamily, in two states: bound to GDP, and to a non-hydrolyzable GTP analog, guanosine-5'-(beta, gamma)-imidotriphosphate (GppNHp). This represents the first structure of a Rab protein bound to GDP. Sec4 in both states grossly resembles other G proteins bound to GDP and GppNHp. In Sec4-GppNHp, structural features common to active Rab proteins are observed. In Sec4-GDP, the switch I region is highly disordered and displaced relative to the switch I region of Ras-GDP. In two of the four molecules of Sec4-GDP in the asymmetric unit of the Sec4-GDP crystals, the switch II region adopts a conformation similar to that seen in the structure of the small G protein Ran bound to GDP. This allows residues threonine 76, glutamate 80, and arginine 81 of Sec4 to make contacts with other conserved residues and water molecules important for nucleotide binding. In the other two molecules in the asymmetric unit, these interactions do not take place. This structural variability in both the switch I and switch II regions of GDP-bound Sec4 provides a possible explanation for the high off-rate of GDP bound to Sec4, and suggests a mechanism for regulation of the GTPase cycle of Rab proteins by GDI proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1G17 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with MG and GNP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1G17 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GNP:'>GNP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G17 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Brunger, A | + | [[Category: Brunger, A T.]] |
[[Category: Stroupe, C.]] | [[Category: Stroupe, C.]] | ||
[[Category: GNP]] | [[Category: GNP]] | ||
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[[Category: g protein rab]] | [[Category: g protein rab]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:44:54 2008'' |
Revision as of 10:44, 21 February 2008
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CRYSTAL STRUCTURE OF SEC4-GUANOSINE-5'-(BETA,GAMMA)-IMIDOTRIPHOSPHATE
Overview
We have determined crystal structures of Sec4, a member of the Rab family in the G protein superfamily, in two states: bound to GDP, and to a non-hydrolyzable GTP analog, guanosine-5'-(beta, gamma)-imidotriphosphate (GppNHp). This represents the first structure of a Rab protein bound to GDP. Sec4 in both states grossly resembles other G proteins bound to GDP and GppNHp. In Sec4-GppNHp, structural features common to active Rab proteins are observed. In Sec4-GDP, the switch I region is highly disordered and displaced relative to the switch I region of Ras-GDP. In two of the four molecules of Sec4-GDP in the asymmetric unit of the Sec4-GDP crystals, the switch II region adopts a conformation similar to that seen in the structure of the small G protein Ran bound to GDP. This allows residues threonine 76, glutamate 80, and arginine 81 of Sec4 to make contacts with other conserved residues and water molecules important for nucleotide binding. In the other two molecules in the asymmetric unit, these interactions do not take place. This structural variability in both the switch I and switch II regions of GDP-bound Sec4 provides a possible explanation for the high off-rate of GDP bound to Sec4, and suggests a mechanism for regulation of the GTPase cycle of Rab proteins by GDI proteins.
About this Structure
1G17 is a Single protein structure of sequence from Saccharomyces cerevisiae with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structures of a Rab protein in its inactive and active conformations., Stroupe C, Brunger AT, J Mol Biol. 2000 Dec 8;304(4):585-98. PMID:11099382
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