1a4r
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1a4r |SIZE=350|CAPTION= <scene name='initialview01'>1a4r</scene>, resolution 2.50Å | |PDB= 1a4r |SIZE=350|CAPTION= <scene name='initialview01'>1a4r</scene>, resolution 2.50Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= | + | |LIGAND= <scene name='pdbligand=GDP:GUANOSINE-5'-DIPHOSPHATE'>GDP</scene>, <scene name='pdbligand=GNH:AMINOPHOSPHONIC+ACID-GUANYLATE+ESTER'>GNH</scene>, <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1a4r FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1a4r OCA], [http://www.ebi.ac.uk/pdbsum/1a4r PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1a4r RCSB]</span> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Vetter, I R.]] | [[Category: Vetter, I R.]] | ||
[[Category: Wittinghofer, A.]] | [[Category: Wittinghofer, A.]] | ||
| - | [[Category: GDP]] | ||
| - | [[Category: GNH]] | ||
| - | [[Category: MG]] | ||
[[Category: gtpase]] | [[Category: gtpase]] | ||
[[Category: hydrolase]] | [[Category: hydrolase]] | ||
[[Category: signal transduction]] | [[Category: signal transduction]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:33:13 2008'' |
Revision as of 15:33, 30 March 2008
| |||||||
| , resolution 2.50Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , , | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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. 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 Sun Mar 30 18:33:13 2008
