1XRI

X-ray structure of a putative phosphoprotein phosphatase from Arabidopsis thaliana gene AT1G05000

Summary for 1XRI

• Entry DOI: 10.2210/pdb1xri/pdb
• Descriptor: At1g05000, SULFATE ION (3 entities in total)
• Functional Keywords: structural genomics, protein structure initiative, psi, cesg, center for eukaryotic structural genomics, at1g05000, phosphoprotein phosphatase, unknown function
• Biological source: Arabidopsis thaliana (thale cress)
• Total number of polymer chains: 2
• Total formula weight: 35464.15

Authors

Wesenberg, G.E.,Smith, D.W.,Phillips Jr., G.N.,Bitto, E.,Bingman, C.A.,Allard, S.T.M.,Center for Eukaryotic Structural Genomics (CESG) (deposition date: 2004-10-14, release date: 2004-10-26, Last modification date: 2024-10-16)

Primary citation

Aceti, D.J.,Bitto, E.,Yakunin, A.F.,Proudfoot, M.,Bingman, C.A.,Frederick, R.O.,Sreenath, H.K.,Vojtik, F.C.,Wrobel, R.L.,Fox, B.G.,Markley, J.L.,Phillips Jr., G.N.
Structural and functional characterization of a novel phosphatase from the Arabidopsis thaliana gene locus At1g05000.
Proteins, 73:241-253, 2008

PubMed 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.

PubMed: 18433060
DOI: 10.1002/prot.22041

Experimental method

X-RAY DIFFRACTION (3.3 Å)