2ntx: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,330,058 edits
No edit summary
Line 1: Line 1:
[[Image:2ntx.gif|left|200px]]
{{Seed}}
[[Image:2ntx.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2ntx|  PDB=2ntx  |  SCENE=  }}  
{{STRUCTURE_2ntx|  PDB=2ntx  |  SCENE=  }}  


'''Prone8'''
===Prone8===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_17218277}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 17218277 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_17218277}}


==About this Structure==
==About this Structure==
Line 20: Line 24:
==Reference==
==Reference==
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:[http://www.ncbi.nlm.nih.gov/pubmed/17218277 17218277]
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:[http://www.ncbi.nlm.nih.gov/pubmed/17218277 17218277]
Purification and crystallization of the catalytic PRONE domain of RopGEF8 and its complex with Rop4 from Arabidopsis thaliana., Thomas C, Weyand M, Wittinghofer A, Berken A, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):607-10. Epub 2006 May 31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16754995 16754995]
[[Category: Arabidopsis thaliana]]
[[Category: Arabidopsis thaliana]]
[[Category: Single protein]]
[[Category: Single protein]]
Line 29: Line 35:
[[Category: Dimer]]
[[Category: Dimer]]
[[Category: Guanine nucleotide exchange factor]]
[[Category: Guanine nucleotide exchange factor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May  4 09:54:24 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 17:49:58 2008''

Revision as of 14:50, 28 July 2008

File:2ntx.png

Template:STRUCTURE 2ntx

Prone8

Template:ABSTRACT PUBMED 17218277

About this Structure

2NTX is a Single protein structure of sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA.

Reference

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

Purification and crystallization of the catalytic PRONE domain of RopGEF8 and its complex with Rop4 from Arabidopsis thaliana., Thomas C, Weyand M, Wittinghofer A, Berken A, Acta Crystallogr Sect F Struct Biol Cryst Commun. 2006 Jun 1;62(Pt, 6):607-10. Epub 2006 May 31. PMID:16754995

Page seeded by OCA on Mon Jul 28 17:49:58 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=2ntx&oldid=709987"