5vjw

Arabidopsis thaliana Rhizobiales-like phosphatase 2 complexed with tungstate

spinqualitylabelsall models 5vjw, resolution 1.80Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 5vjw is a 1 chain structure with sequence from Arabidopsis thaliana. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Method: X-ray diffraction, Resolution 1.8Å Ligands: WO4, ZN Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT Function RLPH2_ARATH Protein phosphatase that dephosphorylates specifically tyrosine-phosphorylated peptides; especially active on dual-phosphorylated substrates containing a phosphothreonine-X-phosphotyrosine motif. Publication Abstract from PubMed Despite belonging to the phosphoserine- and phosphothreonine-specific phosphoprotein phosphatase (PPP) family, Arabidopsis thaliana Rhizobiales-like phosphatase 2 (RLPH2) strongly prefers substrates bearing phosphorylated tyrosine residues. We solved the structures of RLPH2 crystallized in the presence or absence of sodium tungstate. These structures revealed the presence of a central domain that forms a binding site for two divalent metal ions that closely resembles that of other PPP-family enzymes. Unique structural elements from two flanking domains suggest a mechanism for the selective dephosphorylation of phosphotyrosine residues. Cocrystallization with the phosphate mimetic tungstate also suggests how positively charged residues that are highly conserved in the RLPH2 class form an additional pocket that is specific for a phosphothreonine residue located near the phosphotyrosine residue that is bound to the active site. Site-directed mutagenesis confirmed that this auxiliary recognition element facilitates the recruitment of dual-phosphorylated substrates containing a pTxpY motif. Structural basis for the preference of the Arabidopsis thaliana phosphatase RLPH2 for tyrosine-phosphorylated substrates.,Labandera AM, Uhrig RG, Colville K, Moorhead GB, Ng KKS Sci Signal. 2018 Apr 3;11(524). pii: 11/524/eaan8804. doi:, 10.1126/scisignal.aan8804. PMID:29615518 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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