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Structural basis for the preference of the phosphatase RLPH2 for tyrosine-phosphorylated substrates.
Despite belonging to the phosphoserine- and phosphothreonine-specific phosphoprotein phosphatase (PPP) family, -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.
Authors : Labandera Anne-Marie , Uhrig R Glen , Colville Keaton , Moorhead Greg B , Ng Kenneth K S ,
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Pathways :
WP120: Phenylalanine and Tyrosine Biosynthesis
WP1652: Fructose and mannose metabolism
WP1654: gamma-Hexachlorocyclohexane degradation
WP1687: Phenylalanine, tyrosine and tryptophan biosynthesi
WP1696: Riboflavin metabolism
WP1709: Thiamine metabolism
WP1714: Tyrosine metabolism
WP2340: Thiamine (vitamin B1) biosynthesis and salvage
WP2341: vitamin B1 (thiamin) biosynthesis and salvage pathway
WP2349: vitamin B3 (niacin), NAD and NADP biosynthesis pathway
WP2353: vitamin B9 (folate) biosynthesis pathway
WP27: Phenylalanine, Tyrosine, Tryptophan biosynthesis
WP538: Tyrosine Biosynthesis
WP76: TCA Cycle
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Bibliography :
[29615518] Structural basis for the preference of the phosphatase RLPH2 for tyrosine-phosphorylated substrates.
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