1a4r

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spinqualitylabelsall models 1a4r, resolution 2.50Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

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 MG, GDP and GNH 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

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