2y09

The cyanobacterial PP2C-like phosphatase tPphA requires three metals in the catalytic center for efficient catalysis

spinqualitylabelsall models 2y09, resolution 1.70Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2y09 is a 1 chain structure with sequence from Synechococcus elongatus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.7Å Ligands: CA, MG Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function Q8DGS1_THEVB Publication Abstract from PubMed Protein phosphatase M (PPM) regulates key signaling pathways in prokaryotes and eukaryotes. Novel structures of bacterial PPM members revealed three divalent metal ions in their catalytic centers. The function of metal 3 (M3) remained unclear. To reveal its function, we created variants of tPphA from Thermosynechococcus elongatus in all metal-coordinating residues, and multiple variants were created for the M3 coordinating Asp-119 residue. The structures of variants D119A and D193A were resolved, showing loss of M3 binding but unaffected binding of M1 and M2 in the catalytic center of D119A, with the nucleophilic water molecule in the correct place. The catalytic activity of this variant was highly impaired. This and further structure-function analyses showed that M3 is required for catalysis by providing a water molecule as a proton donor during catalysis. Mutation of the homologue Asp residue in human PP2Calpha also caused loss of function, suggesting a general requirement of M3 in PPM-catalyzed reactions. A Third Metal Is Required for Catalytic Activity of the Signal-transducing Protein Phosphatase M tPphA.,Su J, Schlicker C, Forchhammer K J Biol Chem. 2011 Apr 15;286(15):13481-8. Epub 2011 Feb 10. PMID:21310952 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA