1gwn
From Proteopedia
(New page: 200px<br /><applet load="1gwn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1gwn, resolution 2.10Å" /> '''THE CRYSTAL STRUCTUR...) |
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| - | [[Image:1gwn.gif|left|200px]]<br /><applet load="1gwn" size=" | + | [[Image:1gwn.gif|left|200px]]<br /><applet load="1gwn" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1gwn, resolution 2.10Å" /> | caption="1gwn, resolution 2.10Å" /> | ||
'''THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN'''<br /> | '''THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN'''<br /> | ||
==Overview== | ==Overview== | ||
| - | We report the 2.1 A crystal structure of the core G protein domain of the | + | We report the 2.1 A crystal structure of the core G protein domain of the unusual Rho family member RhoE/Rnd3 in complex with endogenous GTP and magnesium. Unlike other small G proteins, RhoE, along with two other proteins Rnd1/Rho6 and Rnd2/RhoN, does not hydrolyze GTP. The main reason for this is the presence of serines in the positions equivalent to Ala59 and Gln61 in Ras. The structure shows that there are still water molecules in similar positions to the waters thought to be involved in the hydrolysis reaction in other G proteins. The structure suggests three not necessarily exclusive explanations for the lack of hydrolysis. The lack of the conserved glutamine raises the energy of the transition state inhibiting hydrolysis. The serines may restrain the waters from moving closer to the GTP, a step that is required to attain the transition state. They also stabilize the GTP-bound conformation of switch II and could prevent conformational changes required during hydrolysis. By superposition of the RhoE structure on structures of Rho family proteins in complex with binding partners, we make predictions on RhoE interactions with these partners. |
==About this Structure== | ==About this Structure== | ||
| - | 1GWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with MG and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1GWN is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus] with <scene name='pdbligand=MG:'>MG</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1GWN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Garavini, H.]] | [[Category: Garavini, H.]] | ||
| - | [[Category: Keep, N | + | [[Category: Keep, N H.]] |
| - | [[Category: Mcalister, M | + | [[Category: Mcalister, M S.B.]] |
| - | [[Category: Phelan, J | + | [[Category: Phelan, J P.]] |
[[Category: Ridley, A.]] | [[Category: Ridley, A.]] | ||
[[Category: Riento, K.]] | [[Category: Riento, K.]] | ||
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[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:54:46 2008'' |
Revision as of 10:54, 21 February 2008
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THE CRYSTAL STRUCTURE OF THE CORE DOMAIN OF RHOE/RND3- A CONSTITUTIVELY ACTIVATED SMALL G PROTEIN
Overview
We report the 2.1 A crystal structure of the core G protein domain of the unusual Rho family member RhoE/Rnd3 in complex with endogenous GTP and magnesium. Unlike other small G proteins, RhoE, along with two other proteins Rnd1/Rho6 and Rnd2/RhoN, does not hydrolyze GTP. The main reason for this is the presence of serines in the positions equivalent to Ala59 and Gln61 in Ras. The structure shows that there are still water molecules in similar positions to the waters thought to be involved in the hydrolysis reaction in other G proteins. The structure suggests three not necessarily exclusive explanations for the lack of hydrolysis. The lack of the conserved glutamine raises the energy of the transition state inhibiting hydrolysis. The serines may restrain the waters from moving closer to the GTP, a step that is required to attain the transition state. They also stabilize the GTP-bound conformation of switch II and could prevent conformational changes required during hydrolysis. By superposition of the RhoE structure on structures of Rho family proteins in complex with binding partners, we make predictions on RhoE interactions with these partners.
About this Structure
1GWN is a Single protein structure of sequence from Mus musculus with and as ligands. Full crystallographic information is available from OCA.
Reference
Crystal structure of the core domain of RhoE/Rnd3: a constitutively activated small G protein., Garavini H, Riento K, Phelan JP, McAlister MS, Ridley AJ, Keep NH, Biochemistry. 2002 May 21;41(20):6303-10. PMID:12009891
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