1a4r
From Proteopedia
(New page: 200px<br /> <applet load="1a4r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1a4r, resolution 2.50Å" /> '''G12V MUTANT OF HUMA...) |
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| - | [[Image:1a4r.gif|left|200px]]<br /> | + | [[Image:1a4r.gif|left|200px]]<br /><applet load="1a4r" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1a4r" size=" | + | |
caption="1a4r, resolution 2.50Å" /> | caption="1a4r, resolution 2.50Å" /> | ||
'''G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM'''<br /> | '''G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The 2.5 A crystal structure of the full length human placental isoform of | + | The 2.5 A crystal structure of the full length human placental isoform of the Gly12 to Val mutant Cdc42 protein (Cdc42(G12V)) bound to both GDP/Mg2+ and GDPNH2 (guanosine-5'-diphospho-beta-amidate) is reported. The crystal contains two molecules in the asymmetric unit, of which one has bound GDP/Mg2+, while the other has bound GDPNH2 without a Mg2+ ion. Crystallization of the protein was induced via hydrolysis of the Cdc42 x GppNHp complex by the presence of contaminating alkaline phosphatase activity in combination with the crystallization conditions. This prompted us to compare the binding characteristics of GDPNH2 vs. GDP. The amino group of GDPNH2 drastically reduces the affinity to Cdc42 in comparison with that of GDP, causes the loss of the Mg2+ ion, and apparently also increases the conformational flexibility of the protein as seen in the crystal. Both the switch I and switch II regions are visible in the electron density of the GDP-bound molecule, but not in the molecule bound to GDPNH2. The C-terminus containing the CaaX-motif is partly ordered in both molecules due to an intramolecular disulfide bond formed between Cys105/Cys188 and Cys305/Cys388, respectively. |
==About this Structure== | ==About this Structure== | ||
| - | 1A4R 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 MG, GDP and GNH as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1A4R 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=MG:'>MG</scene>, <scene name='pdbligand=GDP:'>GDP</scene> and <scene name='pdbligand=GNH:'>GNH</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1A4R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Rudolph, M | + | [[Category: Rudolph, M G.]] |
| - | [[Category: Vetter, I | + | [[Category: Vetter, I R.]] |
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
[[Category: GDP]] | [[Category: GDP]] | ||
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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 11:40:51 2008'' |
Revision as of 09:40, 21 February 2008
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G12V MUTANT OF HUMAN PLACENTAL CDC42 GTPASE IN THE GDP FORM
Overview
The 2.5 A crystal structure of the full length human placental isoform of the Gly12 to Val mutant Cdc42 protein (Cdc42(G12V)) bound to both GDP/Mg2+ and GDPNH2 (guanosine-5'-diphospho-beta-amidate) is reported. The crystal contains two molecules in the asymmetric unit, of which one has bound GDP/Mg2+, while the other has bound GDPNH2 without a Mg2+ ion. Crystallization of the protein was induced via hydrolysis of the Cdc42 x GppNHp complex by the presence of contaminating alkaline phosphatase activity in combination with the crystallization conditions. This prompted us to compare the binding characteristics of GDPNH2 vs. GDP. The amino group of GDPNH2 drastically reduces the affinity to Cdc42 in comparison with that of GDP, causes the loss of the Mg2+ ion, and apparently also increases the conformational flexibility of the protein as seen in the crystal. Both the switch I and switch II regions are visible in the electron density of the GDP-bound molecule, but not in the molecule bound to GDPNH2. The C-terminus containing the CaaX-motif is partly ordered in both molecules due to an intramolecular disulfide bond formed between Cys105/Cys188 and Cys305/Cys388, respectively.
About this Structure
1A4R is a Single protein structure of sequence from Homo sapiens with , and as ligands. Full crystallographic information is available from OCA.
Reference
Nucleotide binding to the G12V-mutant of Cdc42 investigated by X-ray diffraction and fluorescence spectroscopy: two different nucleotide states in one crystal., Rudolph MG, Wittinghofer A, Vetter IR, Protein Sci. 1999 Apr;8(4):778-87. PMID:10211824
Page seeded by OCA on Thu Feb 21 11:40:51 2008
Categories: Homo sapiens | Single protein | Rudolph, M G. | Vetter, I R. | Wittinghofer, A. | GDP | GNH | MG | Gtpase | Hydrolase | Signal transduction
