2nty: Difference between revisions

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New page: left|200px<br /><applet load="2nty" size="450" color="white" frame="true" align="right" spinBox="true" caption="2nty, resolution 3.100Å" /> '''Rop4-GDP-PRONE8'''<...
 
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[[Image:2nty.gif|left|200px]]<br /><applet load="2nty" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:2nty.gif|left|200px]]<br /><applet load="2nty" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="2nty, resolution 3.100&Aring;" />
caption="2nty, resolution 3.100&Aring;" />
'''Rop4-GDP-PRONE8'''<br />
'''Rop4-GDP-PRONE8'''<br />


==Overview==
==Overview==
Rho of plants (Rop) proteins belong to the superfamily of small, GTP-binding (G) proteins and are vital regulators of signal transduction, in plants. In order to become activated, Rop proteins need to exchange GDP, for GTP, an intrinsically slow process catalyzed by guanine nucleotide, exchange factors (GEFs). RopGEFs show no homology to animal RhoGEFs, and, the catalytic mechanism remains elusive. GEF-catalysed nucleotide exchange, proceeds via transient ternary and stable binary complexes. While a number, of structural studies have analyzed binary nucleotide-free G protein-GEF, complexes, very little is known about the ternary complexes. Here we, report the X-ray structure of the catalytic PRONE domain of RopGEF8 from, Arabidopsis thaliana, both alone and in a ternary complex with Rop4 and, GDP. The features of the latter complex, a transient intermediate of the, exchange reaction never directly observed before, suggest a common, mechanism of catalyzed nucleotide exchange applicable to small G proteins, in general.
Rho of plants (Rop) proteins belong to the superfamily of small GTP-binding (G) proteins and are vital regulators of signal transduction in plants. In order to become activated, Rop proteins need to exchange GDP for GTP, an intrinsically slow process catalyzed by guanine nucleotide exchange factors (GEFs). RopGEFs show no homology to animal RhoGEFs, and the catalytic mechanism remains elusive. GEF-catalysed nucleotide exchange proceeds via transient ternary and stable binary complexes. While a number of structural studies have analyzed binary nucleotide-free G protein-GEF complexes, very little is known about the ternary complexes. Here we report the X-ray structure of the catalytic PRONE domain of RopGEF8 from Arabidopsis thaliana, both alone and in a ternary complex with Rop4 and GDP. The features of the latter complex, a transient intermediate of the exchange reaction never directly observed before, suggest a common mechanism of catalyzed nucleotide exchange applicable to small G proteins in general.


==About this Structure==
==About this Structure==
2NTY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with GDP as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2NTY OCA].  
2NTY is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Arabidopsis_thaliana Arabidopsis thaliana] with <scene name='pdbligand=GDP:'>GDP</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NTY OCA].  


==Reference==
==Reference==
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[[Category: complex of prone-gef with rop substrate]]
[[Category: complex of prone-gef with rop substrate]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:10:58 2008''

Revision as of 19:11, 21 February 2008

File:2nty.gif


2nty, resolution 3.100Å

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Rop4-GDP-PRONE8

OverviewOverview

Rho of plants (Rop) proteins belong to the superfamily of small GTP-binding (G) proteins and are vital regulators of signal transduction in plants. In order to become activated, Rop proteins need to exchange GDP for GTP, an intrinsically slow process catalyzed by guanine nucleotide exchange factors (GEFs). RopGEFs show no homology to animal RhoGEFs, and the catalytic mechanism remains elusive. GEF-catalysed nucleotide exchange proceeds via transient ternary and stable binary complexes. While a number of structural studies have analyzed binary nucleotide-free G protein-GEF complexes, very little is known about the ternary complexes. Here we report the X-ray structure of the catalytic PRONE domain of RopGEF8 from Arabidopsis thaliana, both alone and in a ternary complex with Rop4 and GDP. The features of the latter complex, a transient intermediate of the exchange reaction never directly observed before, suggest a common mechanism of catalyzed nucleotide exchange applicable to small G proteins in general.

About this StructureAbout this Structure

2NTY is a Protein complex structure of sequences from Arabidopsis thaliana with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

Structural evidence for a common intermediate in small G protein-GEF reactions., Thomas C, Fricke I, Scrima A, Berken A, Wittinghofer A, Mol Cell. 2007 Jan 12;25(1):141-9. PMID:17218277

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