1dpf: Difference between revisions

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New page: left|200px<br /> <applet load="1dpf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dpf, resolution 2.0Å" /> '''CRYSTAL STRUCTURE OF...
 
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[[Image:1dpf.gif|left|200px]]<br />
[[Image:1dpf.gif|left|200px]]<br /><applet load="1dpf" size="350" color="white" frame="true" align="right" spinBox="true"  
<applet load="1dpf" size="450" color="white" frame="true" align="right" spinBox="true"  
caption="1dpf, resolution 2.0&Aring;" />
caption="1dpf, resolution 2.0&Aring;" />
'''CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP'''<br />
'''CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP'''<br />


==Overview==
==Overview==
Mg(2+) ions are essential for guanosine triphosphatase (GTPase) activity, and play key roles in guanine nucleotide binding and preserving the, structural integrity of GTP-binding proteins. We determined the crystal, structure of a small GTPase RHOA complexed with GDP in the absence of, Mg(2+) at 2.0-A resolution. Elimination of a Mg(2+) ion induces, significant conformational changes in the switch I region that opens up, the nucleotide-binding site. Similar structural changes have been observed, in the switch regions of Ha-Ras bound to its guanine nucleotide exchange, factor, Sos. This RHOA-GDP structure reveals an important regulatory role, for Mg(2+) and suggests that guanine nucleotide exchange factor may, utilize this feature of switch I to produce an open conformation in, GDP/GTP exchange.
Mg(2+) ions are essential for guanosine triphosphatase (GTPase) activity and play key roles in guanine nucleotide binding and preserving the structural integrity of GTP-binding proteins. We determined the crystal structure of a small GTPase RHOA complexed with GDP in the absence of Mg(2+) at 2.0-A resolution. Elimination of a Mg(2+) ion induces significant conformational changes in the switch I region that opens up the nucleotide-binding site. Similar structural changes have been observed in the switch regions of Ha-Ras bound to its guanine nucleotide exchange factor, Sos. This RHOA-GDP structure reveals an important regulatory role for Mg(2+) and suggests that guanine nucleotide exchange factor may utilize this feature of switch I to produce an open conformation in GDP/GTP exchange.


==About this Structure==
==About this Structure==
1DPF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1DPF OCA].  
1DPF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] 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=1DPF OCA].  


==Reference==
==Reference==
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[[Category: protein rhoa-gdp complex]]
[[Category: protein rhoa-gdp complex]]


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Revision as of 13:19, 21 February 2008

File:1dpf.gif


1dpf, resolution 2.0Å

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CRYSTAL STRUCTURE OF A MG-FREE FORM OF RHOA COMPLEXED WITH GDP

OverviewOverview

Mg(2+) ions are essential for guanosine triphosphatase (GTPase) activity and play key roles in guanine nucleotide binding and preserving the structural integrity of GTP-binding proteins. We determined the crystal structure of a small GTPase RHOA complexed with GDP in the absence of Mg(2+) at 2.0-A resolution. Elimination of a Mg(2+) ion induces significant conformational changes in the switch I region that opens up the nucleotide-binding site. Similar structural changes have been observed in the switch regions of Ha-Ras bound to its guanine nucleotide exchange factor, Sos. This RHOA-GDP structure reveals an important regulatory role for Mg(2+) and suggests that guanine nucleotide exchange factor may utilize this feature of switch I to produce an open conformation in GDP/GTP exchange.

About this StructureAbout this Structure

1DPF is a Single protein structure of sequence from Homo sapiens with as ligand. Full crystallographic information is available from OCA.

ReferenceReference

An open conformation of switch I revealed by the crystal structure of a Mg2+-free form of RHOA complexed with GDP. Implications for the GDP/GTP exchange mechanism., Shimizu T, Ihara K, Maesaki R, Kuroda S, Kaibuchi K, Hakoshima T, J Biol Chem. 2000 Jun 16;275(24):18311-7. PMID:10748207

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