Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000.

Proteins
David J AcetiGeorge N Phillips

Abstract

The crystal structure of the protein product of the gene locus At1g05000, a hypothetical protein from A. thaliana, was determined by the multiple-wavelength anomalous diffraction method and was refined to an R factor of 20.4% (R(free) = 24.9%) at 3.3 A. The protein adopts the alpha/beta fold found in cysteine phosphatases, a superfamily of phosphatases that possess a catalytic cysteine and form a covalent thiol-phosphate intermediate during the catalytic cycle. In At1g05000, the analogous cysteine (Cys(150)) is located at the bottom of a positively-charged pocket formed by residues that include the conserved arginine (Arg(156)) of the signature active site motif, HCxxGxxRT. Of 74 model phosphatase substrates tested, purified recombinant At1g05000 showed highest activity toward polyphosphate (poly-P(12-13)) and deoxyribo- and ribonucleoside triphosphates, and less activity toward phosphoenolpyruvate, phosphotyrosine, phosphotyrosine-containing peptides, and phosphatidyl inositols. Divalent metal cations were not required for activity and had little effect on the reaction.

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Citations

Mar 17, 2011·Molecular Genetics and Genomics : MGG·Carlos Romá-MateoRafael Pulido
Nov 4, 2010·Acta Crystallographica. Section F, Structural Biology and Crystallization Communications·Wen YangMark Bartlam
Dec 19, 2012·Biochemistry. Biokhimii︠a︡·A M AvalbaevF M Shakirova
Mar 10, 2016·Acta Crystallographica. Section D, Structural Biology·Thomas C TerwilligerPaul D Adams
Mar 10, 2016·Acta Crystallographica. Section D, Structural Biology·Thomas C TerwilligerPaul D Adams
Sep 12, 2009·FEMS Microbiology Letters·Hyun Sook LeeSung Gyun Kang
Jul 24, 2021·The Biochemical Journal·Henning MühlenbeckCyril Zipfel

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