1dpf

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(New page: 200px<br /> <applet load="1dpf" size="450" color="white" frame="true" align="right" spinBox="true" caption="1dpf, resolution 2.0&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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<applet load="1dpf" size="450" color="white" frame="true" align="right" spinBox="true"
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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==
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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.
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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==
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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].
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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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 16:34:41 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:19:02 2008''

Revision as of 10:19, 21 February 2008


1dpf, resolution 2.0Å

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

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.

About this Structure

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

Reference

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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